6k8w
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of N-domain with NADP of baterial malonyl-CoA reductase== | |
| + | <StructureSection load='6k8w' size='340' side='right'caption='[[6k8w]], [[Resolution|resolution]] 3.17Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6k8w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K8W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K8W FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6k8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k8w OCA], [http://pdbe.org/6k8w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k8w RCSB], [http://www.ebi.ac.uk/pdbsum/6k8w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k8w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6k8w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kim, K J]] | ||
[[Category: Kim, S]] | [[Category: Kim, S]] | ||
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| + | [[Category: Sdr domain]] | ||
Revision as of 09:39, 18 March 2020
Crystal structure of N-domain with NADP of baterial malonyl-CoA reductase
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