4a0s: Difference between revisions
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==STRUCTURE OF THE 2-OCTENOYL-COA CARBOXYLASE REDUCTASE CINF IN COMPLEX WITH NADP AND 2-OCTENOYL-COA== | |||
<StructureSection load='4a0s' size='340' side='right'caption='[[4a0s]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4a0s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_cinnabarigriseus Streptomyces cinnabarigriseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A0S FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO8:OCTANOYL-COENZYME+A'>CO8</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=4a0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0s OCA], [https://pdbe.org/4a0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a0s RCSB], [https://www.ebi.ac.uk/pdbsum/4a0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a0s ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/F0V3Z3_9ACTN F0V3Z3_9ACTN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Polyketides are structurally diverse and medically important natural products that have various biological activities. During biosynthesis, chain elongation uses activated dicarboxylic acid building blocks, and their availability therefore limits side chain variation in polyketides. Recently, the crotonyl-CoA carboxylase-reductase (CCR) class of enzymes was identified in primary metabolism and was found to be involved in extender-unit biosynthesis of polyketides. These enzymes are, in theory, capable of forming dicarboxylic acids that show any side chain from the respective unsaturated fatty acid precursor. To our knowledge, we here report the first crystal structure of a CCR, the hexylmalonyl-CoA synthase from Streptomyces sp. JS360, in complex with its substrate. Structural analysis and biochemical characterization of the enzyme, including active site mutations, are reported. Our analysis reveals how primary metabolic CCRs can evolve to produce various dicarboxylic acid building blocks, setting the stage to use CCRs for the production of unique extender units and, consequently, altered polyketides. | |||
Unusual carbon fixation gives rise to diverse polyketide extender units.,Quade N, Huo L, Rachid S, Heinz DW, Muller R Nat Chem Biol. 2011 Dec 4;8(1):117-24. doi: 10.1038/nchembio.734. PMID:22138621<ref>PMID:22138621</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4a0s" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces cinnabarigriseus]] | |||
[[Category: Heinz DW]] | |||
[[Category: Huo L]] | |||
[[Category: Muller R]] | |||
[[Category: Quade N]] | |||
[[Category: Rachid S]] | |||
Latest revision as of 14:17, 20 December 2023
STRUCTURE OF THE 2-OCTENOYL-COA CARBOXYLASE REDUCTASE CINF IN COMPLEX WITH NADP AND 2-OCTENOYL-COASTRUCTURE OF THE 2-OCTENOYL-COA CARBOXYLASE REDUCTASE CINF IN COMPLEX WITH NADP AND 2-OCTENOYL-COA
Structural highlights
FunctionPublication Abstract from PubMedPolyketides are structurally diverse and medically important natural products that have various biological activities. During biosynthesis, chain elongation uses activated dicarboxylic acid building blocks, and their availability therefore limits side chain variation in polyketides. Recently, the crotonyl-CoA carboxylase-reductase (CCR) class of enzymes was identified in primary metabolism and was found to be involved in extender-unit biosynthesis of polyketides. These enzymes are, in theory, capable of forming dicarboxylic acids that show any side chain from the respective unsaturated fatty acid precursor. To our knowledge, we here report the first crystal structure of a CCR, the hexylmalonyl-CoA synthase from Streptomyces sp. JS360, in complex with its substrate. Structural analysis and biochemical characterization of the enzyme, including active site mutations, are reported. Our analysis reveals how primary metabolic CCRs can evolve to produce various dicarboxylic acid building blocks, setting the stage to use CCRs for the production of unique extender units and, consequently, altered polyketides. Unusual carbon fixation gives rise to diverse polyketide extender units.,Quade N, Huo L, Rachid S, Heinz DW, Muller R Nat Chem Biol. 2011 Dec 4;8(1):117-24. doi: 10.1038/nchembio.734. PMID:22138621[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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