This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
7eqh
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==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. | ||
| + | |||
| + | 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
| |||||||||||
