1v0h: Difference between revisions
New page: left|200px<br /> <applet load="1v0h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v0h, resolution 1.46Å" /> '''ASCOBATE PEROXIDASE... |
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==About this Structure== | ==About this Structure== | ||
1V0H is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Glycine_max Glycine max]] with NA, HEM and SHA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V0H OCA]]. | 1V0H is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Glycine_max Glycine max]] with NA, HEM and SHA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/L-ascorbate_peroxidase L-ascorbate peroxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.11 1.11.1.11]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V0H OCA]]. | ||
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15236572 15236572] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15236572 15236572] | ||
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
[[Category: L-ascorbate peroxidase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Moody, P.C.E.]] | [[Category: Moody, P.C.E.]] | ||
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[[Category: peroxide scavenge]] | [[Category: peroxide scavenge]] | ||
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Revision as of 14:25, 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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