1E4V

Mutant G10V of adenylate kinase from E. coli, modified in the Gly-loop

1E4V の概要

• エントリーDOI: 10.2210/pdb1e4v/pdb
• 関連するPDBエントリー: 1AKE 1ANK 1E4Y 2ECK 4AKE
• 分子名称: Adenylate kinase, BIS(ADENOSINE)-5'-PENTAPHOSPHATE (3 entities in total)
• 機能のキーワード: transferase(phosphotransferase)
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49156.95

構造登録者

Mueller, C.W.,Schulz, G.E. (登録日: 2000-07-12, 公開日: 2000-08-04, 最終更新日: 2024-05-08)

主引用文献

Muller, C.W.,Schulz, G.E.
Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop.
Proteins, 15:42-49, 1993

PubMed Abstract: Two mutants of adenylate kinase from Escherichia coli have been crystallized and analyzed by X-ray diffraction at resolutions of 3.4 and 2.4 A, respectively. These mutants are Pro-9-->Leu and Gly-10-->Val. They were selected for their positions in the highly conserved Gly-loop forming a giant anion hole for the beta-phosphate of ATP (GTP) in adenylate kinases, H-ras-p21, and other nucleotide-binding proteins. Mutants at these positions of H-ras-p21 cause cancer. In adenylate kinase these mutations cause smallish changes at the active site. Relating the structural changes to the known changes in catalysis indicates that these mutants hinder the induced-fit movements. As a side result we find that mutant Pro-9-->Leu and wild-type form one very similar crystal packing contact that is crystallographic in one case and noncrystallographic in the other, while all other packing contacts and the space groups are quite at variance.

PubMed: 8451239
DOI: 10.1002/prot.340150106

実験手法

X-RAY DIFFRACTION (1.85 Å)