title: The structure of human 5-lipoxygenase.
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.
authors.affiliation: Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.
authors.forename: Nathaniel C
authors.initials: NC
authors.lastname: Gilbert
authors.forename: Sue G
authors.initials: SG
authors.lastname: Bartlett
authors.forename: Maria T
authors.initials: MT
authors.lastname: Waight
authors.forename: David B
authors.initials: DB
authors.lastname: Neau
authors.forename: William E
authors.initials: WE
authors.lastname: Boeglin
authors.forename: Alan R
authors.initials: AR
authors.lastname: Brash
authors.forename: Marcia E
authors.initials: ME
authors.lastname: Newcomer
mesh_terms: D000595:Amino Acid Sequence; D001094:Arachidonate 5-Lipoxygenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D006801:Humans; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D050505:Mutant Proteins / Q000737:chemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D050505:Mutant Proteins; D007501:Iron; D001094:Arachidonate 5-Lipoxygenase