6k8v: Difference between revisions

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<StructureSection load='6k8v' size='340' side='right'caption='[[6k8v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6k8v' size='340' side='right'caption='[[6k8v]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6k8v]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K8V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K8V FirstGlance]. <br>
<table><tr><td colspan='2'>[[6k8v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Erythrobacter_dokdonensis_DSW-74 Erythrobacter dokdonensis DSW-74]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6K8V FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2&#8491;</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=6k8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k8v OCA], [http://pdbe.org/6k8v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k8v RCSB], [http://www.ebi.ac.uk/pdbsum/6k8v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k8v ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6k8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k8v OCA], [https://pdbe.org/6k8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6k8v RCSB], [https://www.ebi.ac.uk/pdbsum/6k8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6k8v ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0A1A7BFR5_9SPHN A0A1A7BFR5_9SPHN]
The bi-functional malonyl-CoA reductase is a key enzyme of the 3-hydroxypropionate bi-cycle for bacterial CO2 fixation, catalysing the reduction of malonyl-CoA to malonate semialdehyde and further reduction to 3-hydroxypropionate. Here, we report the crystal structure and the full-length architecture of malonyl-CoA reductase from Porphyrobacter dokdonensis. The malonyl-CoA reductase monomer of 1230 amino acids consists of four tandemly arranged short-chain dehydrogenases/reductases, with two catalytic and two non-catalytic short-chain dehydrogenases/reductases, and forms a homodimer through paring contact of two malonyl-CoA reductase monomers. The complex structures with its cofactors and substrates revealed that the malonyl-CoA substrate site is formed by the cooperation of two short-chain dehydrogenases/reductases and one novel extra domain, while only one catalytic short-chain dehydrogenase/reductase contributes to the formation of the malonic semialdehyde-binding site. The phylogenetic and structural analyses also suggest that the bacterial bi-functional malonyl-CoA has a structural origin that is completely different from the archaeal mono-functional malonyl-CoA and malonic semialdehyde reductase, and thereby constitute an efficient enzyme.
 
Structural insight into bi-functional malonyl-CoA reductase.,Son HF, Kim S, Seo H, Hong J, Lee D, Jin KS, Park S, Kim KJ Environ Microbiol. 2020 Feb;22(2):752-765. doi: 10.1111/1462-2920.14885. Epub, 2019 Dec 20. PMID:31814251<ref>PMID:31814251</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6k8v" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Erythrobacter dokdonensis DSW-74]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kim, K J]]
[[Category: Kim K-J]]
[[Category: Kim, S]]
[[Category: Kim S]]
[[Category: Oxidoreductase]]
[[Category: Sdr domain]]
Retrieved from "https://proteopedia.org/6k8v"