2bov

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spinqualitylabelsall models PDB ID 2bov Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.66Å
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Ligands:	,
Resources:	FirstGlance, OCA, PDBsum, RCSB
Coordinates:	save as pdb, mmCIF, xml

MOLECULAR RECOGNITION OF AN ADP-RIBOSYLATING CLOSTRIDIUM BOTULINUM C3 EXOENZYME BY RALA GTPASE

Overview

C3 exoenzymes (members of the ADP-ribosyltranferase family) are produced by Clostridium botulinum (C3bot1 and -2), Clostridium limosum (C3lim), Bacillus cereus (C3cer), and Staphylococcus aureus (C3stau1-3). These exoenzymes lack a translocation domain but are known to specifically inactivate Rho GTPases in host target cells. Here, we report the crystal structure of C3bot1 in complex with RalA (a GTPase of the Ras subfamily) and GDP at a resolution of 2.66 A. RalA is not ADP-ribosylated by C3 exoenzymes but inhibits ADP-ribosylation of RhoA by C3bot1, C3lim, and C3cer to different extents. The structure provides an insight into the molecular interactions between C3bot1 and RalA involving the catalytic ADP-ribosylating turn-turn (ARTT) loop from C3bot1 and helix alpha4 and strand beta6 (which are not part of the GDP-binding pocket) from RalA. The structure also suggests a molecular explanation for the different levels of C3-exoenzyme inhibition by RalA and why RhoA does not bind C3bot1 in this manner.

About this Structure

2BOV is a Protein complex structure of sequences from Clostridium botulinum and Homo sapiens. This structure supersedes the now removed PDB entry 1WCA. Full crystallographic information is available from OCA.

Reference

Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase., Holbourn KP, Sutton JM, Evans HR, Shone CC, Acharya KR, Proc Natl Acad Sci U S A. 2005 Apr 12;102(15):5357-62. Epub 2005 Apr 4. PMID:15809419

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