1lox

From Proteopedia

Revision as of 14:37, 5 November 2007

RABBIT RETICULOCYTE 15-LIPOXYGENASE

Overview

Here we report the first structure of a mammalian 15-lipoxygenase. The, protein is composed of two domains; a catalytic domain and a previously, unrecognized beta-barrel domain. The N-terminal beta-barrel domain has, topological and sequence identify to a domain in the mammalian lipases, suggesting that these domains may have similar functions in vivo. Within, the C-terminal domain, the lipoxygenase substrate binding site is a, hydrophobic pocket defined by a bound inhibitor. Arachidonic acid can be, docked into this deep hydrophobic pocket with the methyl end extending, down into the bottom of the pocket and the acid end tethered by a, conserved basic residue on the surface of the enzyme. This structure, provides a unifying hypothesis for the positional specificity of mammalian, lipoxygenases.

About this Structure

1LOX is a Single protein structure of sequence from Oryctolagus cuniculus with FE2 and RS7 as ligands. Active as Arachidonate 15-lipoxygenase, with EC number 1.13.11.33 Structure known Active Site: NUL. Full crystallographic information is available from OCA.

Reference

The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity., Gillmor SA, Villasenor A, Fletterick R, Sigal E, Browner MF, Nat Struct Biol. 1997 Dec;4(12):1003-9. PMID:9406550

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