1N6H

Crystal Structure of Human Rab5a

1N6H の概要

• エントリーDOI: 10.2210/pdb1n6h/pdb
• 関連するPDBエントリー: 1N6I 1N6K 1N6L 1N6N 1N6O 1N6P 1N6R
• 分子名称: Ras-related protein Rab-5A, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total)
• 機能のキーワード: rab, gtpase, protein transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Lipid-anchor; Cytoplasmic side (By similarity): P20339
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19612.21

構造登録者

Zhu, G.,Liu, J.,Terzyan, S.,Zhai, P.,Li, G.,Zhang, X.C. (登録日: 2002-11-11, 公開日: 2002-11-27, 最終更新日: 2025-03-26)

主引用文献

Zhu, G.,Liu, J.,Terzyan, S.,Zhai, P.,Li, G.,Zhang, X.C.
High Resolution Crystal Structures of Human Rab5a and Five Mutants with Substitutions in the Catalytically Important Phosphate-Binding Loop
J.Biol.Chem., 278:2452-2460, 2003

PubMed Abstract: GTPase domain crystal structures of Rab5a wild type and five variants with mutations in the phosphate-binding loop are reported here at resolutions up to 1.5 A. Of particular interest, the A30P mutant was crystallized in complexes with GDP, GDP+AlF(3), and authentic GTP, respectively. The other variant crystals were obtained in complexes with a non-hydrolyzable GTP analog, GppNHp. All structures were solved in the same crystal form, providing an unusual opportunity to compare structures of small GTPases with different catalytic rates. The A30P mutant exhibits dramatically reduced GTPase activity and forms a GTP-bound complex stable enough for crystallographic analysis. Importantly, the A30P structure with bound GDP plus AlF(3) has been solved in the absence of a GTPase-activating protein, and it may resemble that of a transition state intermediate. Conformational changes are observed between the GTP-bound form and the transition state intermediate, mainly in the switch II region containing the catalytic Gln(79) residue and independent of A30P mutation-induced local alterations in the P-loop. The structures suggest an important catalytic role for a P-loop backbone amide group, which is eliminated in the A30P mutant, and support the notion that the transition state of GTPase-mediated GTP hydrolysis is of considerable dissociative character.

PubMed: 12433916
DOI: 10.1074/jbc.M211042200

実験手法

X-RAY DIFFRACTION (1.51 Å)