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Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):54-60. Epub 2003 Dec 18.

Refinement of the structure of human Rab5a GTPase domain at 1.05 A resolution.

Author information

  • 1Crystallography Research Program of Oklahoma Medical Research Foundation, 825 NE 13th Street, Oklahoma City, OK 73104, USA. terzyans@omrf.ouhsc.edu

Abstract

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.

PMID:
14684892
[PubMed - indexed for MEDLINE]
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