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Title: 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 1.9 {angstrom} 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.
Authors:
; ; ; ; ;  [1] ;  [2] ;  [2]
  1. (Hebei)
  2. (
Publication Date:
OSTI Identifier:
1038293
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochem. Biophys. Res. Commun.; Journal Volume: 418; Journal Issue: (4) ; 02, 2012
Research Org:
Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
Sponsoring Org:
FOREIGNINDUSTRY
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; CARGO; CHARGE DISTRIBUTION; CRYSTAL STRUCTURE; GTP-ASES; MEMBRANES; PROTEINS; RESOLUTION; SORTING; SWITCHES; TRANSPORT