1r2q
From Proteopedia
Crystal Structure of Human Rab5a GTPase Domain at 1.05 A resolution
Structural highlights
FunctionRAB5A_HUMAN Required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension.[1] 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 PubMedRab5 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Homo sapiens | Large Structures | Li G | Terzyan S | Zhang XC | Zhu G
