2ngr

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spinqualitylabelsall models 2ngr, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

TRANSITION STATE COMPLEX FOR GTP HYDROLYSIS BY CDC42: COMPARISONS OF THE HIGH RESOLUTION STRUCTURES FOR CDC42 BOUND TO THE ACTIVE AND CATALYTICALLY COMPROMISED FORMS OF THE CDC42-GAP.

Overview

The Rho-related small GTP-binding protein Cdc42 has a low intrinsic GTPase, activity that is significantly enhanced by its specific GTPase-activating, protein, Cdc42GAP. In this report, we present the tertiary structure for, the aluminum fluoride-promoted complex between Cdc42 and a catalytically, active domain of Cdc42GAP as well as the complex between Cdc42 and the, catalytically compromised Cdc42GAP(R305A) mutant. These structures, which, mimic the transition state for the GTP hydrolytic reaction, show the, presence of an AIF3 molecule, as was seen for the corresponding, Ras-p120RasGAP complex, but in contrast to what has been reported for the, Rho-Cdc42GAP complex or for heterotrimeric G protein alpha subunits, where, AIF4- was observed. The Cdc42GAP stabilizes both the switch I and switch, II domains of Cdc42 and contributes a highly conserved arginine (Arg 305), to the active site. Comparison of the structures for the wild type and, mutant Cdc42GAP complexes provides important insights into the, GAP-catalyzed GTP hydrolytic reaction.

About this Structure

2NGR is a Protein complex structure of sequences from Homo sapiens with MG, GDP and AF3 as ligands. Full crystallographic information is available from OCA.

Reference

Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP., Nassar N, Hoffman GR, Manor D, Clardy JC, Cerione RA, Nat Struct Biol. 1998 Dec;5(12):1047-52. PMID:9846874

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