2ciw: Difference between revisions
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[[Category: pyrrolidone carboxylic acid]] | [[Category: pyrrolidone carboxylic acid]] | ||
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Revision as of 18:04, 30 October 2007
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CHLOROPEROXIDASE IODIDE COMPLEX
OverviewOverview
Chloroperoxidase (CPO) is a heme-thiolate enzyme that catalyzes hydrogen, peroxide-dependent halogenation reactions. Structural data on substrate, binding have not been available so far. CPO was therefore crystallized in, the presence of iodide or bromide. One halide binding site was identified, at the surface near a narrow channel that connects the surface with the, heme. Two other halide binding sites were identified within and at the, other end of this channel. Together, these sites suggest a pathway for, access of halide anions to the active site. The structure of CPO complexed, with its natural substrate cyclopentanedione was determined at a, resolution of 1.8 A. This is the first example of a CPO structure with a, bound organic substrate. In addition, structures of CPO bound with, ... [(full description)]
About this StructureAbout this Structure
2CIW is a [Single protein] structure of sequence from [Leptoxyphium fumago] with NAG, MAN, MN, IOD and HEM as [ligands]. Active as [Chloride peroxidase], with EC number [1.11.1.10]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate., Kuhnel K, Blankenfeldt W, Terner J, Schlichting I, J Biol Chem. 2006 Aug 18;281(33):23990-8. Epub 2006 Jun 20. PMID:16790441
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