2NGR

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.

Summary for 2NGR

• Entry DOI: 10.2210/pdb2ngr/pdb
• Descriptor: PROTEIN (GTP BINDING PROTEIN (G25K)), PROTEIN (GTPASE ACTIVATING PROTEIN (RHG)), MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: transition state, g-protein, gap, cdc42, alf3., hydrolase
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane ; Lipid-anchor ; Cytoplasmic side : P60953; Cytoplasm: Q07960
• Total number of polymer chains: 2
• Total formula weight: 48286.35

Authors

Nassar, N.,Hoffman, G.,Clardy, J.,Cerione, R. (deposition date: 1998-07-31, release date: 1999-01-06, Last modification date: 2024-10-30)

Primary citation

Nassar, N.,Hoffman, G.R.,Manor, D.,Clardy, J.C.,Cerione, R.A.
Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP.
Nat.Struct.Biol., 5:1047-1052, 1998

PubMed Abstract: 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.

PubMed: 9846874
DOI: 10.1038/4156

Experimental method

X-RAY DIFFRACTION (1.9 Å)