2GIL

Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8 resolution

Summary for 2GIL

• Entry DOI: 10.2210/pdb2gil/pdb
• Descriptor: Ras-related protein Rab-6A, MAGNESIUM ION, GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: protein-nucleotide complex, gtpase-fold, protein transport
• Biological source: Homo sapiens (human)
• Cellular location: Golgi apparatus membrane ; Lipid- anchor . Isoform 1: Golgi apparatus membrane ; Lipid-anchor . Isoform 2: Golgi apparatus membrane ; Lipid-anchor : P20340
• Total number of polymer chains: 4
• Total formula weight: 76666.86

Authors

Bergbrede, T.,Pylypenko, O.,Rak, A.,Alexandrov, K. (deposition date: 2006-03-29, release date: 2006-06-27, Last modification date: 2023-08-30)

Primary citation

Bergbrede, T.,Pylypenko, O.,Rak, A.,Alexandrov, A.
Structure of the extremely slow GTPase Rab6A in the GTP bound form at 1.8 resolution
J.STRUCT.BIOL., 152:235-238, 2005

PubMed Abstract: 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.

PubMed: 16332443
DOI: 10.1016/j.jsb.2005.10.001

Experimental method

X-RAY DIFFRACTION (1.82 Å)