6m09
From Proteopedia
(Difference between revisions)
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==The ligand-free structure of the chloroplast protein At3g03890== | ==The ligand-free structure of the chloroplast protein At3g03890== | ||
| - | <StructureSection load='6m09' size='340' side='right'caption='[[6m09]]' scene=''> | + | <StructureSection load='6m09' size='340' side='right'caption='[[6m09]], [[Resolution|resolution]] 2.10Å' 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=6M09 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6m09]] is a 4 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=6M09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M09 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.101Å</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=6m09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m09 OCA], [https://pdbe.org/6m09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m09 RCSB], [https://www.ebi.ac.uk/pdbsum/6m09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m09 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8LDU1_ARATH Q8LDU1_ARATH] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Plant tetrapyrroles, including heme and bilins, are synthesized in plastids. Heme oxygenase (HO) catalyzes the oxidative cleavage of heme to the linear tetrapyrrole biliverdin as the initial step in bilin biosynthesis. Besides the canonical alpha-helical HO that is conserved from prokaryotes to human, a subfamily of non-canonical dimeric beta-barrel HO has been found in bacteria. In this work, we discovered that the Arabidopsis locus AT3G03890 encodes a dimeric beta-barrel protein that is structurally related to the putative non-canonical HO and is located in chloroplasts. The recombinant protein was able to bind and degrade heme in a manner different from known HO proteins. Crystal structure of the heme-protein complex reveals that the heme-binding site is in the interdimer interface and the heme iron is coordinated by a fixed water molecule. Our results identify a new protein that may function additionally in the tetrapyrrole biosynthetic pathway. | ||
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| + | The Arabidopsis locus AT3G03890 encodes a dimeric beta-barrel protein implicated in heme degradation.,Wang J, Guo Q, Li X, Wang X, Liu L Biochem J. 2020 Dec 7. pii: 227151. doi: 10.1042/BCJ20200712. PMID:33284325<ref>PMID:33284325</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6m09" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Liu L]] | [[Category: Liu L]] | ||
[[Category: Wang J]] | [[Category: Wang J]] | ||
Current revision
The ligand-free structure of the chloroplast protein At3g03890
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