3VTF

Structure of a UDP-glucose dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum

3VTF の概要

• エントリーDOI: 10.2210/pdb3vtf/pdb
• 分子名称: UDP-glucose 6-dehydrogenase, URIDINE-5'-DIPHOSPHATE-GLUCOSE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: two discrete alpha/beta domains, dehydrogenase, oxidoreductase
• 由来する生物種: Pyrobaculum islandicum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48590.21

構造登録者

Sakuraba, H.,Ohshima, T.,Yoneda, K. (登録日: 2012-05-29, 公開日: 2012-09-19, 最終更新日: 2023-11-08)

主引用文献

Sakuraba, H.,Kawai, T.,Yoneda, K.,Ohshima, T.
Structure of a UDP-glucose dehydrogenase from the hyperthermophilic archaeon Pyrobaculum islandicum.
Acta Crystallogr.,Sect.F, 68:1003-1007, 2012

PubMed Abstract: The crystal structure of an extremely thermostable UDP-glucose dehydrogenase (UDP-GDH) from the hyperthermophilic archaeon Pyrobaculum islandicum was determined at a resolution of 2.0 Å. The overall fold was comprised of an N-terminal NAD(+) dinucleotide binding domain and a C-terminal UDP-sugar binding domain connected by a long α-helix, and the main-chain coordinates of the enzyme were similar to those of previously studied UDP-GDHs, including the enzymes from Burkholderia cepacia, Streptococcus pyogenes and Klebsiella pneumoniae. However, the sizes of several surface loops in P. islandicum UDP-GDH were much smaller than the corresponding loops in B. cepacia UDP-GDH but were comparable to those of the S. pyogenes and K. pneumoniae enzymes. Structural comparison revealed that the presence of extensive intersubunit hydrophobic interactions, as well as the formation of an intersubunit aromatic pair network, is likely to be the main factor contributing to the hyperthermostability of P. islandicum UDP-GDH.

PubMed: 22949183
DOI: 10.1107/S1744309112030667

実験手法

X-RAY DIFFRACTION (2 Å)