7eqh
From Proteopedia
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==Crystal structure of Arabidopsis GUN2/HO1 in complex with heme== | ==Crystal structure of Arabidopsis GUN2/HO1 in complex with heme== | ||
| - | <StructureSection load='7eqh' size='340' side='right'caption='[[7eqh]]' scene=''> | + | <StructureSection load='7eqh' size='340' side='right'caption='[[7eqh]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EQH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7eqh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EQH FirstGlance]. <br> |
| - | </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=7eqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eqh OCA], [https://pdbe.org/7eqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eqh RCSB], [https://www.ebi.ac.uk/pdbsum/7eqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eqh ProSAT]</span></td></tr> | + | </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></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=7eqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eqh OCA], [https://pdbe.org/7eqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eqh RCSB], [https://www.ebi.ac.uk/pdbsum/7eqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eqh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HMOX1_ARATH HMOX1_ARATH] Key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Can form complex with heme, is ferredoxin-dependent and its activity is increased in the presence of ascorbate. Plays a role in salt acclimation signaling. May affect the plastid-to-nucleus signaling pathway by perturbing tetrapyrrole synthesis. The plastid-to-nucleus signal plays an important role in the coordinated expression of both nuclear- and chloroplast-localized genes that encode photosynthesis-related proteins.<ref>PMID:10072395</ref> <ref>PMID:10339624</ref> <ref>PMID:11135121</ref> <ref>PMID:11172074</ref> <ref>PMID:12232145</ref> <ref>PMID:12324588</ref> <ref>PMID:12481078</ref> <ref>PMID:16428602</ref> <ref>PMID:19860740</ref> <ref>PMID:20979354</ref> <ref>PMID:21205037</ref> <ref>PMID:7690685</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Arabidopsis thaliana heme oxygenase-1 (AtHO-1), a metabolic enzyme in the heme degradation pathway, serves as a prototype for study of the bilin-related functions in plants. Past biological analyses revealed that AtHO-1 requires ferredoxin-NADP(+) reductase (FNR) and ferredoxin for its enzymatic activity. Here, we characterized the binding and degradation of heme by AtHO-1, and found that ferredoxin is a dispensable component of the reducing system that provides electrons for heme oxidation. Furthermore, we reported the crystal structure of heme-bound AtHO-1, which demonstrates both conserved and previously undescribed features of plant heme oxygenases. Finally, the electron transfer pathway from FNR to AtHO-1 is suggested based on the known structural information. | ||
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| + | Enzymological and structural characterization of Arabidopsis thaliana heme oxygenase-1.,Wang J, Li X, Chang JW, Ye T, Mao Y, Wang X, Liu L FEBS Open Bio. 2022 Sep;12(9):1677-1687. doi: 10.1002/2211-5463.13453. Epub 2022 , Jun 20. PMID:35689519<ref>PMID:35689519</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7eqh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Li X]] | [[Category: Li X]] | ||
[[Category: Liu L]] | [[Category: Liu L]] | ||
[[Category: Wang J]] | [[Category: Wang J]] | ||
Revision as of 10:20, 24 November 2022
Crystal structure of Arabidopsis GUN2/HO1 in complex with heme
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