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PROSITE documentation PDOC51981 |
The RNF213ZNFX1 (RZ)-type zinc finger is found in:
The ubiquitylation of LPS on Salmonella that invade the cytosol relies on the RZ-type zinc finger in the E3 module of RNF213 [1].
The RZ-type zinc finger contains two conserved histidine residues and four conserved cysteine residues in a CHC3H motif. It can bind divalent transition metals, with a preference for Zn(2+). Residues C1, H1, C3, and C4 coordinate the metal ion, whereas C2, not involved in zinc coordination, is the catalytic cysteine nucleophile involved in E2-E3 transthiolation. H2 is located on a flexible loop region adjacent to the loop carrying the active site C2 and might act as a general base that deprotonates the substrate nucleophile [2].
The profile we developed covers the entire RZ-type zinc finger.
Last update:July 2021 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Otten E.G. Werner E. Crespillo-Casado A. Boyle K.B. Dharamdasani V. Pathe C. Santhanam B. Randow F. |
Title | Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection. | |
Source | Nature 594:111-116(2021). | |
PubMed ID | 34012115 | |
DOI | 10.1038/s41586-021-03566-4 |
2 | Authors | Ahel J. Fletcher A. Grabarczyk D.B. Roitinger E. Deszcz L. Lehner A. Virdee S. Clausen T. |
Title | E3 ubiquitin ligase RNF213 employs a non-canonical zinc finger active site and is allosterically regulated by ATP. | |
Source | bioRxiv 0:0-0(2021). | |
DOI | 10.1101/2021.05.10.443411 |