1UKY

SUBSTRATE SPECIFICITY AND ASSEMBLY OF CATALYTIC CENTER DERIVED FROM TWO STRUCTURES OF LIGATED URIDYLATE KINASE

1UKY の概要

• エントリーDOI: 10.2210/pdb1uky/pdb
• 分子名称: URIDYLATE KINASE, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P15700
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23688.42

構造登録者

Mueller-Dieckmann, H.-J.,Schulz, G.E. (登録日: 1994-07-13, 公開日: 1995-01-26, 最終更新日: 2024-10-30)

主引用文献

Muller-Dieckmann, H.J.,Schulz, G.E.
Substrate specificity and assembly of the catalytic center derived from two structures of ligated uridylate kinase.
J.Mol.Biol., 246:522-530, 1995

PubMed Abstract: Two crystal structures of ligated uridylate kinase from Saccharomyces cerevisiae were determined by X-ray analyses. The ligands were ADP and AMP. Cocrystallization with ATP yielded crystals with ADP at the ATP site and a mixture of AMP and ADP at the NMP site. Cocrystallization with ADP gave rise to a distinct crystal type with ADP at the ATP site, but only AMP at the NMP site. In both cases, the substrates are kept in place by favorable crystal contacts. The structures have been refined to R-factors of 17.8% and 19.6% at resolutions of 2.1 A and 1.9 A, respectively. A comparison with the related cytosolic adenylate kinase from pig disclosed large induced-fit movements on substrate binding and the disassembly of the catalytic center in the absence of substrates. The relatively high side-activity of uridylate kinase for AMP is explained by the finding that the binding pocket is sized for an AMP, but constructed to bind UMP together with a water molecule.

PubMed: 7877173
DOI: 10.1006/jmbi.1994.0104

実験手法

X-RAY DIFFRACTION (2.13 Å)