|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH SALICYLHYDROXAMIC ACID== | | ==ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH SALICYLHYDROXAMIC ACID== |
| - | <StructureSection load='1v0h' size='340' side='right' caption='[[1v0h]], [[Resolution|resolution]] 1.46Å' scene=''> | + | <StructureSection load='1v0h' size='340' side='right'caption='[[1v0h]], [[Resolution|resolution]] 1.46Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1v0h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V0H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1v0h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V0H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SHA:SALICYLHYDROXAMIC+ACID'>SHA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.46Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oaf|1oaf]], [[1oag|1oag]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SHA:SALICYLHYDROXAMIC+ACID'>SHA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0h OCA], [https://pdbe.org/1v0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v0h RCSB], [https://www.ebi.ac.uk/pdbsum/1v0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v0h ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0h OCA], [http://pdbe.org/1v0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v0h RCSB], [http://www.ebi.ac.uk/pdbsum/1v0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v0h ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q43758_SOYBN Q43758_SOYBN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 30: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Ascorbate peroxidase|Ascorbate peroxidase]] | + | *[[Ascorbate peroxidase 3D structures|Ascorbate peroxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glycine hispida]] | + | [[Category: Glycine max]] |
| - | [[Category: L-ascorbate peroxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Moody, P C.E]] | + | [[Category: Moody PCE]] |
| - | [[Category: Raven, E L]] | + | [[Category: Raven EL]] |
| - | [[Category: Sharp, K H]] | + | [[Category: Sharp KH]] |
| - | [[Category: Ascorbate peroxidase]]
| + | |
| - | [[Category: Heme peroxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxide scavenge]]
| + | |
| Structural highlights
Function
Q43758_SOYBN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sharp KH, Moody PC, Brown KA, Raven EL. Crystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex. Biochemistry. 2004 Jul 13;43(27):8644-51. PMID:15236572 doi:10.1021/bi049343q
|
