Article ; Online: The structure-function analysis of Obg-like GTPase proteins along the evolutionary tree from bacteria to humans.
Genes to cells : devoted to molecular & cellular mechanisms
2022 Volume 27, Issue 7, Page(s) 469–481
Abstract: Obg proteins belong to P-loop guanine triphosphatase (GTPase) that are conserved from bacteria to humans. Like other GTPases, Obg cycles between guanine triphosphate (GTP) bound "on" state and guanine diphosphate (GDP)-bound "off" state, thereby ... ...
| Abstract | Obg proteins belong to P-loop guanine triphosphatase (GTPase) that are conserved from bacteria to humans. Like other GTPases, Obg cycles between guanine triphosphate (GTP) bound "on" state and guanine diphosphate (GDP)-bound "off" state, thereby controlling various cellular processes. Different members of this group have unique structural characteristics; a conserved glycine-rich N-terminal domain known as obg fold, a central conserved nucleotide binding domain, and a less conserved C-terminal domain of other functions. Obg is a ribosome dependent GTPase helps in ribosome maturation by interacting with several proteins of the 50S subunit of the ribosome. Obg proteins have been widely considered as a regulator of cellular functions, helping in DNA replication, cell division. Apart from that, this protein also takes part in various stress adaptation pathways like a stringent response, sporulation, and general stress response. In this particular review, the structural features of ObgE have been highlighted and how the structure plays important role in interacting with regulators like GTP, ppGpp that are crucial for executing biological function has been orchestrated. In particular, we believe that Obg-like proteins can provide a link between different global pathways that are necessary for fine-tuning cellular processes to maintain the cellular energy status. |
|---|---|
| MeSH term(s) | Amino Acid Sequence ; Bacteria ; Bacterial Proteins/metabolism ; GTP Phosphohydrolases/metabolism ; Guanine ; Guanosine Triphosphate/metabolism ; Humans |
| Chemical Substances | Bacterial Proteins ; Guanine (5Z93L87A1R) ; Guanosine Triphosphate (86-01-1) ; GTP Phosphohydrolases (EC 3.6.1.-) |
| Language | English |
| Publishing date | 2022-05-24 |
| Publishing country | England |
| Document type | Journal Article ; Review |
| ZDB-ID | 1330000-3 |
| ISSN | 1365-2443 ; 1356-9597 |
| ISSN (online) | 1365-2443 |
| ISSN | 1356-9597 |
| DOI | 10.1111/gtc.12942 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
Full text online
More links
Kategorien
In stock of ZB MED Cologne/Königswinter
| Zs.A 4539: 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) |
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.