3O8Y

Stable-5-Lipoxygenase

Summary for 3O8Y

• Entry DOI: 10.2210/pdb3o8y/pdb
• Descriptor: Arachidonate 5-lipoxygenase, FE (II) ION (3 entities in total)
• Functional Keywords: plat, lox, dioxygenase, coactosin like protein, five lipoxygenase activating protein, nuclear membrane, cytosol, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P09917
• Total number of polymer chains: 2
• Total formula weight: 158984.17

Authors

Newcomer, M.E.,Gilbert, N.C.,Bartlett, S.G.,Waight, M.T.,Neau, D.B.,Boeglin, W.E.,Brash, A.R. (deposition date: 2010-08-03, release date: 2011-01-19, Last modification date: 2024-02-21)

Primary citation

Gilbert, N.C.,Bartlett, S.G.,Waight, M.T.,Neau, D.B.,Boeglin, W.E.,Brash, A.R.,Newcomer, M.E.
The structure of human 5-lipoxygenase.
Science, 331:217-219, 2011

PubMed 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.

PubMed: 21233389
DOI: 10.1126/science.1197203

Experimental method

X-RAY DIFFRACTION (2.389 Å)