The structure of human 5-lipoxygenase

  • Science. 2011 Jan 14;331(6014):217-9. doi: 10.1126/science.1197203.
Nathaniel C Gilbert  1 ,  Sue G Bartlett ,  Maria T Waight ,  David B Neau ,  William E Boeglin ,  Alan R Brash ,  Marcia E Newcomer
Affiliations
  • 1. Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.
PMID: 21233389 DOI: 10.1126/science.1197203
Abstract

The synthesis of both proinflammatory leukotrienes and anti-inflammatory lipoxins requires the enzyme 5-lipoxygenase (5-LOX). 5-LOX activity is short-lived, apparently in part because of an intrinsic instability of the enzyme. We identified a 5-LOX-specific destabilizing sequence that is involved in orienting the carboxyl terminus, which binds the catalytic iron. Here, we report the crystal structure at 2.4 angstrom resolution of human 5-LOX stabilized by replacement of this sequence.