1v0h: Difference between revisions
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Revision as of 17:12, 30 October 2007
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ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH SALICYLHYDROXAMIC ACID
OverviewOverview
Ascorbate peroxidase is a bifunctional peroxidase that catalyzes the, H(2)O(2)-dependent oxidation of both ascorbate and various aromatic, substrates. The ascorbate binding site was recently identified as being, close to the gamma-heme edge [Sharp, K. H., Mewies, M., Moody, P. C. E., and Raven, E. L. (2003)Nat. Struct. Biol. 10, 303-307]. In this work, the, X-ray crystal structure of recombinant soybean cytosolic ascorbate, peroxidase (rsAPX) in complex with salicylhydroxamic acid (SHA) has been, determined to 1.46 A. The SHA molecule is bound close to the delta-heme, edge in a cavity that connects the distal side of the heme to the surface, of the protein. There are hydrogen bonds between the phenolic hydroxide of, the SHA and the main chain carbonyl of Pro132, between the carbonyl ... [(full description)]
About this StructureAbout this Structure
1V0H is a [Single protein] structure of sequence from [Glycine max] with NA, HEM and SHA as [ligands]. Active as [L-ascorbate peroxidase], with EC number [1.11.1.11]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex., Sharp KH, Moody PC, Brown KA, Raven EL, Biochemistry. 2004 Jul 13;43(27):8644-51. PMID:15236572
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