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Article ; Online: Crystal structures of UDP-N-acetylmuramic acid L-alanine ligase (MurC) from Mycobacterium bovis with and without UDP-N-acetylglucosamine.

Seo, Pil Won / Park, Suk Youl / Hofmann, Andreas / Kim, Jeong Sun

Acta crystallographica. Section D, Structural biology

2021 Volume 77, Issue Pt 5, Page(s) 618–627

Abstract: ... in its biosynthesis represent promising targets for the development of novel antibacterial drugs. Here, the crystal ... by the MurA and MurB enzymes, an amino acid is added to UNAM by UDP-N-acetylmuramic acid L-alanine ligase ...

Abstract	Peptidoglycan comprises repeating units of N-acetylmuramic acid, N-acetylglucosamine and short cross-linking peptides. After the conversion of UDP-N-acetylglucosamine (UNAG) to UDP-N-acetylmuramic acid (UNAM) by the MurA and MurB enzymes, an amino acid is added to UNAM by UDP-N-acetylmuramic acid L-alanine ligase (MurC). As peptidoglycan is an essential component of the bacterial cell wall, the enzymes involved in its biosynthesis represent promising targets for the development of novel antibacterial drugs. Here, the crystal structure of Mycobacterium bovis MurC (MbMurC) is reported, which exhibits a three-domain architecture for the binding of UNAM, ATP and an amino acid as substrates, with a nickel ion at the domain interface. The ATP-binding loop adopts a conformation that is not seen in other MurCs. In the UNAG-bound structure of MbMurC, the substrate mimic interacts with the UDP-binding domain of MbMurC, which does not invoke rearrangement of the three domains. Interestingly, the glycine-rich loop of the UDP-binding domain of MbMurC interacts through hydrogen bonds with the glucose moiety of the ligand, but not with the pyrophosphate moiety. These findings suggest that UNAG analogs might serve as potential candidates for neutralizing the catalytic activity of bacterial MurC.
MeSH term(s)	Acetylglucosamine/metabolism ; Bacterial Proteins/chemistry ; Ligases/chemistry ; Mycobacterium bovis/enzymology ; Protein Binding ; Protein Conformation ; Substrate Specificity
Chemical Substances	Bacterial Proteins ; Ligases (EC 6.-) ; Acetylglucosamine (V956696549)
Language	English
Publishing date	2021-04-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	2968623-4
ISSN	2059-7983 ; 0907-4449
ISSN (online)	2059-7983
ISSN	0907-4449
DOI	10.1107/S2059798321002199
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Article: Partial charge transfer in the salt co-crystal of l-ascorbic acid and 4,4'-bi-pyridine.

Sylvester, Eric / McGovern, Mitchell / Young Lee, An / Nguyen, Phanxico / Park, Jungeun / Benedict, Jason B

Acta crystallographica. Section E, Crystallographic communications

2019 Volume 75, Issue Pt 6, Page(s) 728–731

Abstract: In the title 1:2 co-crystal, C ...

Abstract	In the title 1:2 co-crystal, C
Language	English
Publishing date	2019-05-03
Publishing country	England
Document type	Journal Article
ZDB-ID	2041947-8
ISSN	2056-9890 ; 1600-5368
ISSN	2056-9890 ; 1600-5368
DOI	10.1107/S2056989019005334
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Article ; Online: Partial charge transfer in the salt co-crystal of l-ascorbic acid and 4,4′-bipyridine

Eric Sylvester / Mitchell McGovern / An Young Lee / Phanxico Nguyen / Jungeun Park / Jason B. Benedict

Acta Crystallographica Section E: Crystallographic Communications, Vol 75, Iss 6, Pp 728-

2019 Volume 731

Abstract: In the title 1:2 co-crystal, C10H9N2+·(C6H7.75O6·C6H7.25O6)−, l-ascorbic acid (LAA) and 4,4 ... previously published co-crystal of LAA and 3-bromo-4-pyridone is presented. ... bipyridine (BPy) co-crystallize in the chiral space group P21 with two molecules of LAA, and one molecule ...

Abstract	In the title 1:2 co-crystal, C10H9N2+·(C6H7.75O6·C6H7.25O6)−, l-ascorbic acid (LAA) and 4,4′-bipyridine (BPy) co-crystallize in the chiral space group P21 with two molecules of LAA, and one molecule of bpy in the asymmetric unit. The structure was modeled in two parts due to possible proton transfer from LAA to the corresponding side of the bpy molecule having an occupancy of approximately 0.25 and part 2 with an occupancy of approximately 0.75. In this structure, LAA forms hydrogen bonds with neighboring LAA molecules, forming extended sheets of LAA molecules which are bridged by bpy molecules. A comparison to a related and previously published co-crystal of LAA and 3-bromo-4-pyridone is presented.
Keywords	crystal structure ; co-crystal ; charge transfer ; L-ascorbic acid ; 4,4′-bipyridine ; Chemistry ; QD1-999
Language	English
Publishing date	2019-06-01T00:00:00Z
Publisher	International Union of Crystallography
Document type	Article ; Online
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Article ; Online: Crystallization and preliminary X-ray crystallographic studies of dehydroascorbate reductase (DHAR) from Oryza sativa L. japonica.

Do, Hackwon / Kim, Il-Sup / Kim, Young-Saeng / Shin, Sun-Young / Kim, Jin-Ju / Mok, Ji-Eun / Park, Seong-Im / Wi, Ah Ram / Park, Hyun / Kim, Han-Woo / Yoon, Ho-Sung / Lee, Jun Hyuck

Acta crystallographica. Section F, Structural biology communications

2014 Volume 70, Issue Pt 6, Page(s) 781–785

Abstract: ... and increases the yield of rice grains. However, the crystal structure and detailed mechanisms ... diffraction data indicated that the crystal contained one OsDHAR molecule in the asymmetric unit and belonged ... crystallized using the sitting-drop vapour-diffusion method at pH 8.0 and 298 K. Plate-shaped crystals were ...

Abstract	Dehydroascorbate reductase from Oryza sativa L. japonica (OsDHAR), a key enzyme in the regeneration of vitamin C, maintains reduced pools of ascorbic acid to detoxify reactive oxygen species. In previous studies, the overexpression of OsDHAR in transgenic rice increased grain yield and biomass as well as the amount of ascorbate, suggesting that ascorbate levels are directly associated with crop production in rice. Hence, it has been speculated that the increased level of antioxidants generated by OsDHAR protects rice from oxidative damage and increases the yield of rice grains. However, the crystal structure and detailed mechanisms of this important enzyme need to be further elucidated. In this study, recombinant OsDHAR protein was purified and crystallized using the sitting-drop vapour-diffusion method at pH 8.0 and 298 K. Plate-shaped crystals were obtained using 0.15 M potassium bromide, 30%(w/v) PEG MME 2000 as a precipitant, and the crystals diffracted to a resolution of 1.9 Å on beamline 5C at the Pohang Accelerator Laboratory. The X-ray diffraction data indicated that the crystal contained one OsDHAR molecule in the asymmetric unit and belonged to space group P2₁ with unit-cell parameters a=47.03, b=48.38, c=51.83 Å, β=107.41°.
MeSH term(s)	Amino Acid Sequence ; Crystallography, X-Ray ; Molecular Sequence Data ; Oryza/enzymology ; Oxidoreductases/chemistry ; Sequence Homology, Amino Acid
Chemical Substances	Oxidoreductases (EC 1.-) ; glutathione dehydrogenase (ascorbate) (EC 1.8.5.1)
Language	English
Publishing date	2014-05-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2053-230X
ISSN (online)	2053-230X
DOI	10.1107/S2053230X14009133
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Article: Meaning Making Following Trauma.

Park, Crystal L

Frontiers in psychology

2022 Volume 13, Page(s) 844891

Language	English
Publishing date	2022-03-23
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2563826-9
ISSN	1664-1078
ISSN	1664-1078
DOI	10.3389/fpsyg.2022.844891
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Article ; Online: Crystal structure of the GluR0 ligand-binding core from Nostoc punctiforme in complex with L-glutamate: structural dissection of the ligand interaction and subunit interface.

Lee, Jun Hyuck / Kang, Gil Bu / Lim, Hyun-Ho / Jin, Kyeong Sik / Kim, Se-Hwan / Ree, Moonhor / Park, Chul-Seung / Kim, Soon-Jong / Eom, Soo Hyun

Journal of molecular biology

2008 Volume 376, Issue 2, Page(s) 308–316

Abstract: ... of the ionotropic glutamate receptor (iGluR). We have solved the crystal structure of the ligand-binding core of NpGluR0 in complex ... with l-glutamate at a resolution of 2.1 A. The structure exhibits a noncanonical ligand interaction and ... with the gamma-carboxyl group of bound L-glutamate: in GluR0 from Synechocystis (SGluR0) and other iGluRs ...

Abstract	GluR0 from Nostoc punctiforme (NpGluR0) is a bacterial homologue of the ionotropic glutamate receptor (iGluR). We have solved the crystal structure of the ligand-binding core of NpGluR0 in complex with l-glutamate at a resolution of 2.1 A. The structure exhibits a noncanonical ligand interaction and two distinct subunit interfaces. The side-chain guanidium group of Arg80 forms a salt bridge with the gamma-carboxyl group of bound L-glutamate: in GluR0 from Synechocystis (SGluR0) and other iGluRs, the equivalent residues are Asn or Thr, which cannot form a similar interaction. We suggest that the local positively charged environment and the steric constraint created by Arg80 mediate the selectivity of L-glutamate binding by preventing the binding of positively charged and hydrophobic amino acids. In addition, the NpGluR0 ligand-binding core forms a new subunit interface in which the two protomers are arranged differently than the known iGluR and SGluR0 dimer interfaces. The significance of there being two different dimer interfaces was investigated using analytical ultracentrifugation analysis.
MeSH term(s)	Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Binding Sites ; Conserved Sequence ; Crystallography, X-Ray ; Dimerization ; Glutamic Acid/genetics ; Glutamic Acid/metabolism ; Hydrogen Bonding ; Ligands ; Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Molecular Weight ; Nostoc/chemistry ; Nostoc/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Receptors, Glutamate/chemistry ; Receptors, Glutamate/genetics ; Receptors, Glutamate/metabolism ; Recombinant Proteins/metabolism ; Sequence Homology, Amino Acid ; Ultracentrifugation
Chemical Substances	Bacterial Proteins ; Ligands ; Protein Subunits ; Receptors, Glutamate ; Recombinant Proteins ; Glutamic Acid (3KX376GY7L)
Language	English
Publishing date	2008-02-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2007.10.081
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Article ; Online: Crystallization and preliminary X-ray crystallographic analysis of L-rhamnose isomerase with a novel high thermostability from Bacillus halodurans.

Doan, Thi-Ngoc-Thanh / Prabhu, Ponnandy / Kim, Jin-Kwang / Ahn, Yeh-Jin / Natarajan, Sampath / Kang, Lin-Woo / Park, Geon Tae / Lim, Sang-Boem / Lee, Jung-Kul

Acta crystallographica. Section F, Structural biology and crystallization communications

2010 Volume 66, Issue Pt 6, Page(s) 677–680

Abstract: ... in order to elucidate the molecular basis of its unique enzymatic properties. The crystals were grown ... L-Rhamnose isomerases catalyze isomerization between L-rhamnose (6-deoxy-L-mannose) and L ... rhamnulose (6-deoxy-L-fructose), which is the first step in rhamnose catabolism. L-Rhamnose isomerase ...

Abstract	L-Rhamnose isomerases catalyze isomerization between L-rhamnose (6-deoxy-L-mannose) and L-rhamnulose (6-deoxy-L-fructose), which is the first step in rhamnose catabolism. L-Rhamnose isomerase from Bacillus halodurans ATCC BAA-125 (BHRI) exhibits interesting characteristics such as high thermostability and selective substrate specificity. BHRI fused with an HHHHHH sequence was purified and crystallized in order to elucidate the molecular basis of its unique enzymatic properties. The crystals were grown by the hanging-drop vapour-diffusion method and belonged to the monoclinic space group P2(1), with unit-cell parameters a = 83.2, b = 164.9, c = 92.0 A, beta = 116.0 degrees . Diffraction data were collected to 2.5 A resolution. According to a Matthews coefficient calculation, there are four monomers in the asymmetric unit with a V(M) of 3.0 A(3) Da(-1) and a solvent content of 59.3%. The initial structure of BHRI has been determined by the molecular-replacement method.
MeSH term(s)	Aldose-Ketose Isomerases/chemistry ; Bacillus/enzymology ; Crystallization ; Crystallography, X-Ray ; Enzyme Stability ; Temperature
Chemical Substances	Aldose-Ketose Isomerases (EC 5.3.1.-) ; L-rhamnose isomerase (EC 5.3.1.14)
Language	English
Publishing date	2010-05-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1744-3091
ISSN (online)	1744-3091
DOI	10.1107/S174430911001256X
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Book: Medical illness and positive life change

Park, Crystal L.

can crisis lead to personal transformation?

(Decade of behavior series)

2009

Author's details	ed. by Crystal L. Park
Series title	Decade of behavior series
Keywords	Life Change Events ; Adaptation, Psychological ; Personality Development ; Sick/Psychology ; Life change events ; Clinical health psychology ; Self-actualization (Psychology) ; Krankheit ; Lebenskrise ; Persönlichkeitsentfaltung
Subject	Persönlichkeit ; Freie Persönlichkeitsentfaltung ; Freie Entfaltung der Persönlichkeit ; Kritisches Lebensereignis ; Erkrankung ; Krankheitszustand ; Krankheiten ; Morbus ; Nosos ; Pathos
Subject code	616.0019
Language	English
Size	XV, 261 S. : Ill., graph. Darst., 26cm
Publisher	American Psychological Assoc
Publishing place	Washington, DC u.a.
Publishing country	United States
Document type	Book
Note	Overview of theoretical perspectives / Crystal L. Park -- Challenges to assessing positive life change / Howard Tennen & Glenn Affleck -- Example statistical strategy for assessing positive life change among individuals with breast cancer / Charles S. Carver, Suzanne C. Lechner, and Michael H. Antoni -- Benefit finding among children and adolescents with diabetes / Vicki S. Helgeson, Lindsey Lopez, and Constance Mennella -- Lifespan developmental perspectives on stress-related growth / Carolyn M. Aldwin, Michael R. Levenson, and Linda Kelly -- Lessons learned about benefit finding among individuals with cancer or HIV/AIDS / Suzanne C. Lechner and Kathryn E. Weaver -- Illness perceptions and benefit finding among individuals with breast cancer, acoustic neuroma, or heart disease / Keith J. Petrie and Arden Corter -- Positive life change and the social context of illness: an expanded social-cognitive processing model / Stephen J. Lepore and William Kernan -- Biological correlates: how psychological components of benefit finding may lead to physiological benefits / Julienne E. Bower, Elissa Epel, and Judith Tedlie Moskowitz -- Is benefit finding good for individuals with chronic disease? / Sara B. Algoe and Annette L. Stanton -- Enhancing positive adaptation: example intervention during treatment for breast cancer / Michael H. Antoni, Charles S. Carver, and Suzanne C. Lechner -- The clinician as expert companion / Richard G. Tedeschi and Lawrence G. Calhoun. - Includes bibliographical references and index. - Formerly CIP
HBZ-ID	HT015797693
ISBN	978-1-4338-0396-3 ; 1-4338-0396-8
Database	Catalogue ZB MED Medicine, Health

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Shelf mark	Loan status	Location
2009 A 674	order for loan	Magazin

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Book: Trauma, meaning, and spirituality

Park, Crystal L. / Currier, Joseph M. / Harris, J. Irene / Slattery, Jeanne M.

translating research into clinical practice

2017

Author's details	Crystal L. Park, Joseph M. Currier, J. Irene Harris and Jeanne M. Slattery
Keywords	Trauma and Stressor Related Disorders / psychology ; Spirituality ; Models, Psychological ; Counseling / methods
Language	English
Edition	First edition
Publisher	American Psychological Association
Publishing place	Washington, DC
Publishing country	United States
Document type	Book
HBZ-ID	HT019199712
ISBN	978-1-4338-2325-1 ; 1-4338-2325-X
Database	Catalogue ZB MED Medicine, Health

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2017 A 199	available for loan (reading room)	Lesesaal EG

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Article: Photosensor and Photocatalytic Activities of the L-Glycine Capped ZnS:Mn Nanocrystals in Aqueous Solution.

Park, Jinwoo / Choi, Mi / Hwang, Cheong-Soo

Journal of nanoscience and nanotechnology

2018 Volume 18, Issue 9, Page(s) 6137–6141

Abstract: ... synthesized by capping the surface with L-glycine molecules at various pH conditions. The UV-Visible and ... In this study, water-dispersible manganese (II) ion-doped ZnS nanocrystals (ZnS:Mn NCs) were ...

Abstract	In this study, water-dispersible manganese (II) ion-doped ZnS nanocrystals (ZnS:Mn NCs) were synthesized by capping the surface with L-glycine molecules at various pH conditions. The UV-Visible and solution photoluminescence (PL) spectra showed broad peaks approximately at 330 and 590 nm, respectively. The calculated relative quantum efficiencies were in the range of 4.9∼5.8%, and the average particle sizes measured from the HR-TEM images were about 8 nm. Moreover, the surface charges of the corresponding ZnS:Mn-Gly NCs were determined by the electrophoretic method as: (-)14.8 mV (pH 2), (-)9.5 mV (pH 5), and (-)6.4 mV (pH 10) respectively. The most negatively charged ZnS:Mn-Gly-pH 2 NCs were applied as a fluorescence sensor to detect copper (II) ions in water by an exclusive luminescence quenching effect. In addition, photocatalytic activity of the ZnS:Mn-Gly-pH 2 NCs was also evaluated by measuring the degradation rate of an organic dye (methylene blue, MB) molecule under the UV light irradiation. The ZnS:Mn-Gly-pH 2 NCs showed the photodegradation efficiency of the MB molecule with a pseudo-first-order reaction constant (kobs) of 4.3 × 10-4 min-1, which is higher than those of other amino acids-capped ZnS:Mn NCs at the same conditions.
Language	English
Publishing date	2018-02-14
Publishing country	United States
Document type	Journal Article
ISSN	1533-4880
ISSN	1533-4880
DOI	10.1166/jnn.2018.15618
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