2gwl
From Proteopedia
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{{STRUCTURE_2gwl| PDB=2gwl | SCENE= }} | {{STRUCTURE_2gwl| PDB=2gwl | SCENE= }} | ||
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===Crystal structure of the Salmonella SpvB ATR Domain in complex with NADH=== | ===Crystal structure of the Salmonella SpvB ATR Domain in complex with NADH=== | ||
+ | {{ABSTRACT_PUBMED_16905096}} | ||
- | + | ==Function== | |
+ | [[http://www.uniprot.org/uniprot/SPVB_SALCH SPVB_SALCH]] Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin on 'Arg-177'. ADP-ribosylation prevents the polymerization of G-actin to F-actin, causing actin filament depolymerization, destruction of the cytoskeleton and cytotoxicity. Does not possess NAD(+)-glycohydrolase activity, unlike most mART enzymes (By similarity). | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:016905096</ref><references group="xtra"/> | + | <ref group="xtra">PMID:016905096</ref><references group="xtra"/><references/> |
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | [[Category: Salmonella enterica subsp. enterica serovar typhimurium]] | ||
[[Category: Margarit, S M.]] | [[Category: Margarit, S M.]] |
Revision as of 08:28, 30 October 2013
Contents |
Crystal structure of the Salmonella SpvB ATR Domain in complex with NADH
Template:ABSTRACT PUBMED 16905096
Function
[SPVB_SALCH] Mono-ADP-ribosylates eukaryotic muscle and non-muscle actin on 'Arg-177'. ADP-ribosylation prevents the polymerization of G-actin to F-actin, causing actin filament depolymerization, destruction of the cytoskeleton and cytotoxicity. Does not possess NAD(+)-glycohydrolase activity, unlike most mART enzymes (By similarity).
About this Structure
2gwl is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar typhimurium. Full crystallographic information is available from OCA.
Reference
- Margarit SM, Davidson W, Frego L, Stebbins CE. A steric antagonism of actin polymerization by a salmonella virulence protein. Structure. 2006 Aug;14(8):1219-29. PMID:16905096 doi:10.1016/j.str.2006.05.022