Journal
SCIENCE
Volume 331, Issue 6014, Pages 217-219Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1197203
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Funding
- American Heart Association [MCB 08553920E]
- NSF [0818387]
- NIH [GM-15431]
- Louisiana Governors' Biotechnology Initiative
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0818387] Funding Source: National Science Foundation
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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.
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