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| | <StructureSection load='1we1' size='340' side='right'caption='[[1we1]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1we1' size='340' side='right'caption='[[1we1]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1we1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WE1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WE1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1we1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WE1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1we1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1we1 OCA], [http://pdbe.org/1we1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1we1 RCSB], [http://www.ebi.ac.uk/pdbsum/1we1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1we1 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=1we1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1we1 OCA], [https://pdbe.org/1we1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1we1 RCSB], [https://www.ebi.ac.uk/pdbsum/1we1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1we1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HO1_SYNY3 HO1_SYNY3]] Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae (By similarity). | + | [https://www.uniprot.org/uniprot/HO1_SYNY3 HO1_SYNY3] Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae (By similarity). |
| | == 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: Heme oxygenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fukuyama, K]] | + | [[Category: Synechocystis sp. PCC 6803]] |
| - | [[Category: Migita, C T]] | + | [[Category: Fukuyama K]] |
| - | [[Category: Sugishima, M]] | + | [[Category: Migita CT]] |
| - | [[Category: Yoshida, T]] | + | [[Category: Sugishima M]] |
| - | [[Category: Zhang, X]] | + | [[Category: Yoshida T]] |
| - | [[Category: Oxidoreductase]]
| + | [[Category: Zhang X]] |
| Structural highlights
Function
HO1_SYNY3 Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae (By similarity).
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
Heme oxygenase (HO) catalyzes the oxidative degradation of heme utilizing molecular oxygen and reducing equivalents. In photosynthetic organisms, HO functions in the biosynthesis of such open-chain tetrapyrroles as phyto-chromobilin and phycobilins, which are involved in the signal transduction for light responses and light harvesting for photosynthesis, respectively. We have determined the first crystal structure of a HO-1 from a photosynthetic organism, Synechocystis sp. PCC 6803 (Syn HO-1), in complex with heme at 2.5 A resolution. Heme-Syn HO-1 shares a common folding with other heme-HOs. Although the heme pocket of heme-Syn HO-1 is, for the most part, similar to that of mammalian HO-1, they differ in such features as the flexibility of the distal helix and hydrophobicity. In addition, 2-propanol derived from the crystallization solution occupied the hydrophobic cavity, which is proposed to be a CO trapping site in rat HO-1 that suppresses product inhibition. Although Syn HO-1 and mammalian HO-1 are similar in overall structure and amino acid sequence (57% similarity vs. human HO-1), their molecular surfaces differ in charge distribution. The surfaces of the heme binding sides are both positively charged, but this patch of Syn HO-1 is narrow compared to that of mammalian HO-1. This feature is suited to the selective binding of ferredoxin, the physiological redox partner of Syn HO-1; the molecular size of ferredoxin is approximately 10 kDa whereas the size of NADPH-cytochrome P450 reductase, a reducing partner of mammalian HO-1, is approximately 77 kDa. A docking model of heme-Syn HO-1 and ferredoxin suggests indirect electron transfer from an iron-sulfur cluster in ferredoxin to the heme iron of heme-Syn HO-1.
Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme.,Sugishima M, Migita CT, Zhang X, Yoshida T, Fukuyama K Eur J Biochem. 2004 Nov;271(22):4517-25. PMID:15560792[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sugishima M, Migita CT, Zhang X, Yoshida T, Fukuyama K. Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme. Eur J Biochem. 2004 Nov;271(22):4517-25. PMID:15560792 doi:http://dx.doi.org/10.1111/j.1432-1033.2004.04411.x
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