3VTF

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

Summary for 3VTF

• Entry DOI: 10.2210/pdb3vtf/pdb
• Descriptor: UDP-glucose 6-dehydrogenase, URIDINE-5'-DIPHOSPHATE-GLUCOSE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: two discrete alpha/beta domains, dehydrogenase, oxidoreductase
• Biological source: Pyrobaculum islandicum
• Total number of polymer chains: 1
• Total formula weight: 48590.21

Authors

Sakuraba, H.,Ohshima, T.,Yoneda, K. (deposition date: 2012-05-29, release date: 2012-09-19, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)