2GIL

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

2GIL の概要

• エントリーDOI: 10.2210/pdb2gil/pdb
• 分子名称: Ras-related protein Rab-6A, MAGNESIUM ION, GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: protein-nucleotide complex, gtpase-fold, protein transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Golgi apparatus membrane ; Lipid- anchor . Isoform 1: Golgi apparatus membrane ; Lipid-anchor . Isoform 2: Golgi apparatus membrane ; Lipid-anchor : P20340
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 76666.86

構造登録者

Bergbrede, T.,Pylypenko, O.,Rak, A.,Alexandrov, K. (登録日: 2006-03-29, 公開日: 2006-06-27, 最終更新日: 2023-08-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.82 Å)