Download MendeleyRefinement of the structure of human Rab5a GTPase domain at 1.05 A resolution.
Terzyan, S., Zhu, G., Li, G., Zhang, X.C.(2004) Acta Crystallogr D Biol Crystallogr 60: 54-60
- PubMed: 14684892
- DOI: https://doi.org/10.1107/s0907444903021632
- Primary Citation of Related Structures:
1R2Q - PubMed 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.
Organizational Affiliation:
Crystallography Research Program of Oklahoma Medical Research Foundation, 825 NE 13th Street, Oklahoma City, OK 73104, USA. [email protected]
