Article ; Online: Protein yoga: Conformational versatility of the Hemolysin II C-terminal domain detailed by NMR structures for multiple states.
Protein science : a publication of the Protein Society
2021 Volume 30, Issue 5, Page(s) 990–1005
Abstract: The C-terminal domain of Bacillus cereus hemolysin II (HlyIIC), stabilizes the trans-membrane-pore ... P405, and structurally adjacent loops. Thermodynamic linkage analysis shows that at 25 C the cis ...
| Abstract | The C-terminal domain of Bacillus cereus hemolysin II (HlyIIC), stabilizes the trans-membrane-pore formed by the HlyII toxin and may aid in target cell recognition. Initial efforts to determine the NMR structure of HlyIIC were hampered by cis/trans isomerization about the single proline at position 405 that leads to doubling of NMR resonances. We used the mutant P405M-HlyIIC that eliminates the cis proline to determine the NMR structure of the domain, which revealed a novel fold. Here, we extend earlier studies to the NMR structure determination of the cis and trans states of WT-HlyIIC that exist simultaneously in solution. The primary structural differences between the cis and trans states are in the loop that contains P405, and structurally adjacent loops. Thermodynamic linkage analysis shows that at 25 C the cis proline, which already has a large fraction of 20% in the unfolded protein, increases to 50% in the folded state due to coupling with the global stability of the domain. The P405M or P405A substitutions eliminate heterogeneity due to proline isomerization but lead to the formation of a new dimeric species. The NMR structure of the dimer shows that it is formed through domain-swapping of strand β5, the last segment of secondary structure following P405. The presence of P405 in WT-HlyIIC strongly disfavors the dimer compared to the P405M-HlyIIC or P405A-HlyIIC mutants. The WT proline may thus act as a "gatekeeper," warding off aggregative misfolding. |
|---|---|
| MeSH term(s) | Amino Acid Substitution ; Bacillus cereus/chemistry ; Bacillus cereus/genetics ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Hemolysin Proteins/chemistry ; Hemolysin Proteins/genetics ; Mutation, Missense ; Nuclear Magnetic Resonance, Biomolecular ; Protein Domains |
| Chemical Substances | ApxII toxin, bacteria ; Bacterial Proteins ; Hemolysin Proteins |
| Language | English |
| Publishing date | 2021-03-30 |
| Publishing country | United States |
| Document type | Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. |
| ZDB-ID | 1106283-6 |
| ISSN | 1469-896X ; 0961-8368 |
| ISSN (online) | 1469-896X |
| ISSN | 0961-8368 |
| DOI | 10.1002/pro.4066 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
Full text online
More links
Kategorien
In stock of ZB MED Cologne/Königswinter
| Zs.A 3407: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG) |
|||
| Zs.MO 1: Show issues |
Order via subito
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.