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| <StructureSection load='1iyn' size='340' side='right'caption='[[1iyn]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='1iyn' size='340' side='right'caption='[[1iyn]], [[Resolution|resolution]] 1.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1iyn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/American_tobacco American tobacco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IYN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1iyn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IYN 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></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]] 1.6Å</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='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></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=1iyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyn OCA], [http://pdbe.org/1iyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iyn RCSB], [http://www.ebi.ac.uk/pdbsum/1iyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyn ProSAT]</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=1iyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iyn OCA], [https://pdbe.org/1iyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iyn RCSB], [https://www.ebi.ac.uk/pdbsum/1iyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iyn ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q8LNY5_TOBAC Q8LNY5_TOBAC] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: American tobacco]] | |
- | [[Category: L-ascorbate peroxidase]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Nakamura, Y]] | + | [[Category: Nicotiana tabacum]] |
- | [[Category: Tada, T]] | + | [[Category: Nakamura Y]] |
- | [[Category: Wada, K]] | + | [[Category: Tada T]] |
- | [[Category: Ascorbate]] | + | [[Category: Wada K]] |
- | [[Category: Hydrogen peroxide]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Peroxidase]]
| + | |
- | [[Category: Stromal ascorbate peroxidase]]
| + | |
- | [[Category: Tobacco plant]]
| + | |
| Structural highlights
Function
Q8LNY5_TOBAC
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 (APX) is a heme-containing protein that plays a central role in scavenging H(2)O(2) in higher plants. The structure of stromal APX (sAPX) was determined at 1.6 A to an R-factor of 19.1% and an R-free-factor of 22.3%. The electrostatic potential of the gamma-channel that connects the molecular surface of sAPX to the gamma-edge of heme was more positive than that of cytosolic APX (cAPX) from pea, so sAPX might bind more easily with ascorbate than cAPX. The overall structure of sAPX was similar to those of cAPX from pea and cytochrome c peroxidase (CCP) from yeast, with a substantial difference in a loop structure located in the vicinity of the heme. The side chain of Arg169 in sAPX corresponding to His169 in cAPX and His181 in CCP extended in the opposite direction from the heme, forming two hydrogen bonds with carbonyl groups in the loop structure. The rapid inactivation of sAPX might be due to the characteristic conformation of Arg169 owing to the loop structure of sAPX.
Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights into its instability.,Wada K, Tada T, Nakamura Y, Ishikawa T, Yabuta Y, Yoshimura K, Shigeoka S, Nishimura K J Biochem. 2003 Aug;134(2):239-44. PMID:12966073[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wada K, Tada T, Nakamura Y, Ishikawa T, Yabuta Y, Yoshimura K, Shigeoka S, Nishimura K. Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights into its instability. J Biochem. 2003 Aug;134(2):239-44. PMID:12966073
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