1CTQ

STRUCTURE OF P21RAS IN COMPLEX WITH GPPNHP AT 100 K

1CTQ の概要

• エントリーDOI: 10.2210/pdb1ctq/pdb
• 関連するPDBエントリー: 1QRA
• 分子名称: PROTEIN (TRANSFORMING PROTEIN P21/H-RAS-1), MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: g protein, gtp hydrolysis, kinetic crystallography, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane. Isoform 2: Nucleus: P01112
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19421.69

構造登録者

Scheidig, A.,Burmester, C.,Goody, R.S. (登録日: 1999-08-20, 公開日: 1999-11-15, 最終更新日: 2023-08-09)

主引用文献

Scheidig, A.J.,Burmester, C.,Goody, R.S.
The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins.
Structure Fold.Des., 7:1311-1324, 1999

PubMed Abstract: In numerous biological events the hydrolysis of guanine triphosphate (GTP) is a trigger to switch from the active to the inactive protein form. In spite of the availability of several high-resolution crystal structures, the details of the mechanism of nucleotide hydrolysis by GTPases are still unclear. This is partly because the structures of the proteins in their active states had to be determined in the presence of non-hydrolyzable GTP analogues (e.g. GppNHp). Knowledge of the structure of the true Michaelis complex might provide additional insights into the intrinsic protein hydrolysis mechanism of GTP and related nucleotides.

PubMed: 10574788
DOI: 10.1016/S0969-2126(00)80021-0

実験手法

X-RAY DIFFRACTION (1.26 Å)