Skip to main content
padlock icon - secure page this page is secure

Structure of a UDP‐glucose dehydrogenase from the hyperthermophilic archaeon

Buy Article:

$52.00 + tax (Refund Policy)

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.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Document Type: Research Article

Publication date: September 1, 2012

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more