Crystal structure of inactive form of Rab3B

Wei Zhang; Yang Shen; Ronghong Jiao; Yanli Liu; Lingfu Deng; Chao Qi

doi:10.1016/j.bbrc.2012.01.124

Crystal structure of inactive form of Rab3B

Biochem Biophys Res Commun. 2012 Feb 24;418(4):841-4. doi: 10.1016/j.bbrc.2012.01.124. Epub 2012 Jan 31.

Authors

Wei Zhang¹, Yang Shen, Ronghong Jiao, Yanli Liu, Lingfu Deng, Chao Qi

Affiliation

¹ Hubei Key Laboratory of Genetic Regulation and Integrative Biology, College of Life Science, Huazhong Normal University, Wuhan 430079, PR China.

PMID: 22321395
DOI: 10.1016/j.bbrc.2012.01.124

Abstract

Rab proteins are the largest family of ras-related GTPases in eukaryotic cells. They act as directional molecular switches at membrane trafficking, including vesicle budding, cargo sorting, transport, tethering, and fusion. Here, we generated and crystallized the Rab3B:GDP complex. The structure of the complex was solved to 1.9Å resolution and the structural base comparison with other Rab3 members provides a structural basis for the GDP/GTP switch in controlling the activity of small GTPase. The comparison of charge distribution among the members of Rab3 also indicates their different roles in vesicular trafficking.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Crystallography, X-Ray
Guanosine Diphosphate / chemistry*
Humans
Molecular Sequence Data
Protein Structure, Secondary
rab3 GTP-Binding Proteins / chemistry*

Substances

Guanosine Diphosphate
RAB3B protein, human
rab3 GTP-Binding Proteins