Affordable Access

Publisher Website

Structural Basis of Phospholipase Activity ofStaphylococcus hyicuslipase

Authors
Journal
Journal of Molecular Biology
0022-2836
Publisher
Elsevier
Publication Date
Volume
371
Issue
2
Identifiers
DOI: 10.1016/j.jmb.2007.05.041
Keywords
  • Staphylococcus Hyicuslipase
  • Phospholipase
  • Substrate Specificity
  • Alpha/Beta Hydrolase Fold
  • Crystal Structure
Disciplines
  • Chemistry
  • Medicine

Abstract

Abstract Staphylococcus hyicus lipase differs from other bacterial lipases in its high phospholipase A 1 activity. Here, we present the crystal structure of the S. hyicus lipase at 2.86 Å resolution. The lipase is in an open conformation, with the active site partly covered by a neighbouring molecule. Ser124, Asp314 and His355 form the catalytic triad. The substrate-binding cavity contains two large hydrophobic acyl chain-binding pockets and a shallow and more polar third pocket that is capable of binding either a (short) fatty acid or a phospholipid head-group. A model of a phospholipid bound in the active site shows that Lys295 is at hydrogen bonding distance from the substrate's phosphate group. Residues Ser356, Glu292 and Thr294 hold the lysine in position by hydrogen bonding and electrostatic interactions. These observations explain the biochemical data showing the importance of Lys295 and Ser356 for phospholipid binding and phospholipase A 1 activity.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

The phospholipase activity ofStaphylococcus hyicus...

on Chemistry and Physics of Lipid... Jan 01, 1998

Structural basis of phospholipase activity of Stap...

on Journal of Molecular Biology Aug 10, 2007

Structural basis of the significant calmodulin-ind...

on Protein Engineering Design and... June 2010

Lipid peroxidation and phospholipase A2 activity i...

on Biochimica et Biophysica Acta Aug 12, 1988
More articles like this..