5u4u

pseudoGTPase domain (pG1) of p190RhoGAP-A

spinqualitylabelsall models 5u4u, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5u4u is a 1 chain structure with sequence from Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: MLI, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1L8F832_XENLA Publication Abstract from PubMed The two p190RhoGAP proteins, p190RhoGAP-A and -B, are key regulators of Rho GTPase signaling and are essential for actin cytoskeletal structure and contractility. Here we report the discovery of two evolutionarily conserved GTPase-like domains located in the 'middle domain', previously thought to be unstructured. Deletion of these domains reduces RhoGAP activity. Crystal structures, MANT-GTPgammaS binding, thermal denaturation, biochemical assays and sequence homology analysis all strongly support defects in nucleotide-binding activity. Analysis of p190RhoGAP proteins therefore indicates the presence of two previously unidentified domains which represent an emerging group of pseudoenzymes, the pseudoGTPases.A growing number of 'pseudoenzymes' with a regulatory role in signal transduction processes but without catalytic activity are being identified. Here, the authors identify two pseudoGTPase domains in p190RhoGAP, characterize them biochemically and structurally and show that they influence RhoGAP activity. p190RhoGAP proteins contain pseudoGTPase domains.,Stiegler AL, Boggon TJ Nat Commun. 2017 Sep 11;8(1):506. doi: 10.1038/s41467-017-00483-x. PMID:28894085 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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