1R2Q

Crystal Structure of Human Rab5a GTPase Domain at 1.05 A resolution

Summary for 1R2Q

• Entry DOI: 10.2210/pdb1r2q/pdb
• Related: 1N6H 1N6I 1N6K 1N6L 1N6N
• Descriptor: Ras-related protein Rab-5A, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total)
• Functional Keywords: rab, gtpase, gnp, atomic resolution, protein transport
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Lipid-anchor; Cytoplasmic side (By similarity): P20339
• Total number of polymer chains: 1
• Total formula weight: 20086.64

Authors

Terzyan, S.,Zhu, G.,Li, G.,Zhang, X.C. (deposition date: 2003-09-29, release date: 2003-12-23, Last modification date: 2023-08-23)

Primary citation

Terzyan, S.,Zhu, G.,Li, G.,Zhang, X.C.
Refinement of the structure of human Rab5a GTPase domain at 1.05 A resolution.
Acta Crystallogr.,Sect.D, 60:54-60, 2004

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.

PubMed: 14684892
DOI: 10.1107/S0907444903021632

Experimental method

X-RAY DIFFRACTION (1.05 Å)