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| <StructureSection load='7cka' size='340' side='right'caption='[[7cka]], [[Resolution|resolution]] 1.06Å' scene=''> | | <StructureSection load='7cka' size='340' side='right'caption='[[7cka]], [[Resolution|resolution]] 1.06Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7cka]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CKA FirstGlance]. <br> | | <table><tr><td colspan='2'>[[7cka]] 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=7CKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CKA FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.06Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HO1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine hispida])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=7cka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cka OCA], [https://pdbe.org/7cka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cka RCSB], [https://www.ebi.ac.uk/pdbsum/7cka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cka 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=7cka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cka OCA], [https://pdbe.org/7cka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cka RCSB], [https://www.ebi.ac.uk/pdbsum/7cka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cka ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/I1JW65_SOYBN I1JW65_SOYBN] |
| Heme oxygenase (HO) converts heme to carbon monoxide, biliverdin, and free iron, products that are essential in cellular redox signaling and iron recycling. In higher plants, HO is also involved in the biosynthesis of photoreceptor pigment precursors. Despite many common enzymatic reactions, the amino acid sequence identity between plant-type and other HOs is exceptionally low ( approximately 19.5%), and amino acids that are catalytically important in mammalian HO are not conserved in plant-type HOs. Structural characterization of plant-type HO is limited to spectroscopic characterization by electron spin resonance, and it remains unclear how the structure of plant-type HO differs from that of other HOs. Here, we have solved the crystal structure of Glycine max (soybean) HO-1 (GmHO-1) at a resolution of 1.06 A and carried out the isothermal titration calorimetry measurements and NMR spectroscopic studies of its interaction with ferredoxin, the plant-specific electron donor. The high-resolution X-ray structure of GmHO-1 reveals several novel structural components: an additional irregularly structured region, a new water tunnel from the active site to the surface, and a hydrogen-bonding network unique to plant-type HOs. Structurally important features in other HOs, such as His ligation to the bound heme, are conserved in GmHO-1. Based on combined data from X-ray crystallography, isothermal titration calorimetry, and NMR measurements, we propose the evolutionary fine-tuning of plant-type HOs for ferredoxin dependency in order to allow adaptation to dynamic pH changes on the stroma side of the thylakoid membrane in chloroplast without losing enzymatic activity under conditions of fluctuating light.
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| Crystal structure of higher plant heme oxygenase-1 and its mechanism of interaction with ferredoxin.,Tohda R, Tanaka H, Mutoh R, Zhang X, Lee YH, Konuma T, Ikegami T, Migita CT, Kurisu G J Biol Chem. 2020 Dec 24;296:100217. doi: 10.1074/jbc.RA120.016271. PMID:33839679<ref>PMID:33839679</ref>
| | ==See Also== |
| | | *[[Heme oxygenase 3D structures|Heme oxygenase 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7cka" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Glycine hispida]] | | [[Category: Glycine max]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Kurisu, G]] | | [[Category: Kurisu G]] |
| [[Category: Tanaka, H]] | | [[Category: Tanaka H]] |
| [[Category: Tohda, R]] | | [[Category: Tohda R]] |
| [[Category: Metal binding protein]]
| |
| [[Category: Oxidoreductase]]
| |