1lox
From Proteopedia
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| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Arachidonate 15-lipoxygenase, with EC number 1.13.11.33 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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