1r2q

Crystal Structure of Human Rab5a GTPase Domain at 1.05 A resolution

spinqualitylabelsall models 1r2q, resolution 1.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1r2q is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.05Å Ligands: GNP, GOL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RAB5A_HUMAN Required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Rab5 is a GTPase that regulates early endosome fusion. Its GTPase domain crystal structure is reported here at 1.05 A resolution in complex with a GTP-analog molecule. It provides the highest resolution three-dimensional model so far obtained for proteins from the Ras-like GTPase family. This study allows extension of structural examination of the GTPase machinery as well as of high-resolution protein structures in general. For example, a buried water-molecule network was observed underneath the switch regions, which is consistent with the functional roles of these regions in the molecular-switching process. Furthermore, residues of multiple conformation and clustered distribution of anisotropic thermal motions of the protein molecule may have general implications for the function of Ras-like GTPases. Refinement of the structure of human Rab5a GTPase domain at 1.05 A resolution.,Terzyan S, Zhu G, Li G, Zhang XC Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):54-60. Epub 2003, Dec 18. PMID:14684892 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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