Crystal structure of inactive form of Rab3B.
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.
Hubei Key Laboratory of Genetic Regulation and Integrative Biology, College of Life Science, Huazhong Normal University, Wuhan 430079, PR China.
Wei
W
Zhang
Yang
Y
Shen
Ronghong
R
Jiao
Yanli
Y
Liu
Lingfu
L
Deng
Chao
C
Qi
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D006153:Guanosine Diphosphate / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D020692:rab3 GTP-Binding Proteins / Q000737:chemistry*
D006153:Guanosine Diphosphate; C492131:RAB3B protein, human; D020692:rab3 GTP-Binding Proteins