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

Structure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae

Buy Article:

$52.00 + tax (Refund Policy)

Saccharomyces cerevisiae Hsp33/YOR391Cp is a member of the ThiI/DJ‐1/PfpI superfamily. Hsp33 was overexpressed in Escherichia coli and its crystal structure was determined at 2.40 Å resolution. Structural comparison revealed that Hsp33 adopts an α/β‐hydrolase fold and possesses the putative Cys–His–Glu catalytic triad common to the Hsp31 family, suggesting that Hsp33 and Hsp31 share similar aminopeptidase activity, while structural deviations in helices α2–α3 of the core domain might be responsible for the access of different peptide substrates.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: Hsp33/YOR391Cp; Saccharomyces cerevisiae; ThiI/DJ‐1/PfpI superfamily

Document Type: Research Article

Affiliations: Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China

Publication date: December 1, 2010

  • 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
X
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