Structural highlights
Function
RAB6A_HUMAN Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Has a low GTPase activity.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Rab/Ypt GTPases represent a>60 member large family of membrane traffic regulators in eukaryotic cells. Members of this group display intrinsic GTPase activity varying over two orders of magnitude. Here, we show that Rab6A represents the RabGTPase with the slowest spontaneous GTPase activity yet measured (5x10(-6)s(-1)). Due to the very low intrinsic hydrolysis rate we were able to crystallise and solve the structure of the Rab6A:GTP complex to 1.82A resolution. Analysis of the structure suggests that low catalytic activity of the Rab6A might be due to high flexibility of the Switch II region and a low degree of constraint of critically important for catalysis Gln 72.
Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8A resolution.,Bergbrede T, Pylypenko O, Rak A, Alexandrov K J Struct Biol. 2005 Dec;152(3):235-8. Epub 2005 Nov 18. PMID:16332443[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bergbrede T, Pylypenko O, Rak A, Alexandrov K. Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8A resolution. J Struct Biol. 2005 Dec;152(3):235-8. Epub 2005 Nov 18. PMID:16332443 doi:10.1016/j.jsb.2005.10.001
