2HUR

Escherichia coli nucleoside diphosphate kinase

2HUR の概要

• エントリーDOI: 10.2210/pdb2hur/pdb
• 関連するPDBエントリー: 1NPK 2NCK
• 分子名称: NUCLEOSIDE DIPHOSPHATE KINASE, SULFATE ION (3 entities in total)
• 機能のキーワード: type ii tetramer, signaling protein, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0A763
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 92677.63

構造登録者

Moynie, L.,Giraud, M.-F.,Georgescauld, F.,Lascu, I.,Dautant, A. (登録日: 2006-07-27, 公開日: 2007-04-10, 最終更新日: 2023-08-30)

主引用文献

Moynie, L.,Giraud, M.-F.,Georgescauld, F.,Lascu, I.,Dautant, A.
The structure of the Escherichia coli nucleoside diphosphate kinase reveals a new quaternary architecture for this enzyme family
Proteins, 67:755-765, 2007

PubMed Abstract: Nucleoside diphosphate kinase (NDPK) catalyzes the transfer of gamma-phosphate from nucleoside triphosphates to nucleoside diphosphates. The subunit folding and the dimeric basic structural unit are remarkably the same for available structures but, depending on species, dimers self-associate to form hexamers or tetramers. The crystal structure of the Escherichia coli NDPK reveals a new tetrameric quaternary structure for this protein family. The two tetramers differ by the relative orientation of interacting dimers, which face either the convex or the concave side of their central sheet as in either Myxococcus xanthus (type I) or E. coli (type II), respectively. In the type II tetramer, the subunits interact by a new interface harboring a zone called the Kpn loop as in hexamers, but by the opposite face of this loop. The evolutionary conservation of the interface residues indicates that this new quaternary structure seems to be the most frequent assembly mode in bacterial tetrameric NDP kinases.

PubMed: 17330300
DOI: 10.1002/prot.21316

実験手法

X-RAY DIFFRACTION (1.62 Å)