1v0h: Difference between revisions
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[[Image:1v0h.gif|left|200px]]<br /><applet load="1v0h" size=" | [[Image:1v0h.gif|left|200px]]<br /><applet load="1v0h" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1v0h, resolution 1.46Å" /> | caption="1v0h, resolution 1.46Å" /> | ||
'''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH SALICYLHYDROXAMIC ACID'''<br /> | '''ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH SALICYLHYDROXAMIC ACID'''<br /> | ||
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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/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] Known structural/functional Site: <scene name='pdbsite=AC1:Sha Binding Site For Chain X'>AC1</scene>. Full crystallographic information is available from [http:// | 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 <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=SHA:'>SHA</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Sha+Binding+Site+For+Chain+X'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0H OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: peroxide scavenge]] | [[Category: peroxide scavenge]] | ||
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Revision as of 11:13, 3 February 2008
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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 oxygen, of SHA and the side chain guanadinium group of Arg38, and between the, hydroxamic acid group and the indole nitrogen of Trp41. The structure, provides the first information about the location of the aromatic binding, site in ascorbate peroxidase and, together with our previous data [Sharp, K. H., et al. (2003) Nat. Struct. Biol. 10, 303-307], completes the, structural description of the binding properties of ascorbate peroxidase., The mechanistic implications of the results are discussed in terms of our, current understanding of how APX catalyzes oxidation of different types of, substrates bound at different locations.
About this StructureAbout this Structure
1V0H is a Single protein structure of sequence from Glycine max with , and as ligands. Active as L-ascorbate peroxidase, with EC number 1.11.1.11 Known structural/functional Site: . 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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