2FE4

The crystal structure of human neuronal Rab6B in its inactive GDP-bound form

Summary for 2FE4

• Entry DOI: 10.2210/pdb2fe4/pdb
• Related: 2FFQ
• Descriptor: Ras-related protein Rab-6B, MAGNESIUM ION, NITRATE ION, ... (5 entities in total)
• Functional Keywords: protein-nucleotide complex, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Golgi apparatus membrane; Lipid-anchor: Q9NRW1
• Total number of polymer chains: 1
• Total formula weight: 20322.95

Authors

Garcia-Saez, I.,Tcherniuk, F.,Kozielski, F. (deposition date: 2005-12-15, release date: 2006-07-04, Last modification date: 2024-02-14)

Primary citation

Garcia-Saez, I.,Tcherniuk, S.,Kozielski, F.
The structure of human neuronal Rab6B in the active and inactive form.
Acta Crystallogr.,Sect.D, 62:725-733, 2006

PubMed Abstract: The Rab small G-protein family plays important roles in eukaryotes as regulators of vesicle traffic. In Rab proteins, the hydrolysis of GTP to GDP is coupled with association with and dissociation from membranes. Conformational changes related to their different nucleotide states determine their effector specificity. The crystal structure of human neuronal Rab6B was solved in its 'inactive' (with bound MgGDP) and 'active' (MgGTPgammaS-bound) forms to 2.3 and 1.8 A, respectively. Both crystallized in space group P2(1)2(1)2(1), with similar unit-cell parameters, allowing the comparison of both structures without packing artifacts. Conformational changes between the inactive GDP and active GTP-like state are observed mainly in the switch I and switch II regions, confirming their role as a molecular switch. Compared with other Rab proteins, additional changes are observed in the Rab6 subfamily-specific RabSF3 region that might contribute to the specificity of Rab6 for its different effector proteins.

PubMed: 16790928
DOI: 10.1107/S0907444906015319

Experimental method

X-RAY DIFFRACTION (2.3 Å)