6owe

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<StructureSection load='6owe' size='340' side='right'caption='[[6owe]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
<StructureSection load='6owe' size='340' side='right'caption='[[6owe]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6owe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Kitsk Kitsk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OWE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OWE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6owe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_setae_KM-6054 Kitasatospora setae KM-6054]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OWE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=N9V:5-O-[(S)-{[(S)-[(3R)-4-({(1E)-3-[(2-{[(2S)-2-carboxybutanoyl]sulfanyl}ethyl)amino]-3-oxoprop-1-en-1-yl}amino)-3-hydroxy-2,2-dimethyl-4-oxobutoxy](hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]adenosine+3-(dihydrogen+phosphate)'>N9V</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ccr1, KSE_56510 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=452652 KITSK])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=N9V:5-O-[(S)-{[(S)-[(3R)-4-({(1E)-3-[(2-{[(2S)-2-carboxybutanoyl]sulfanyl}ethyl)amino]-3-oxoprop-1-en-1-yl}amino)-3-hydroxy-2,2-dimethyl-4-oxobutoxy](hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]adenosine+3-(dihydrogen+phosphate)'>N9V</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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<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=6owe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6owe OCA], [http://pdbe.org/6owe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6owe RCSB], [http://www.ebi.ac.uk/pdbsum/6owe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6owe ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6owe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6owe OCA], [https://pdbe.org/6owe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6owe RCSB], [https://www.ebi.ac.uk/pdbsum/6owe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6owe ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/E4N096_KITSK E4N096_KITSK]
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Carboxylases are biocatalysts that capture and convert carbon dioxide (CO2) under mild conditions and atmospheric concentrations at a scale of more than 400 Gt annually. However, how these enzymes bind and control the gaseous CO2 molecule during catalysis is only poorly understood. One of the most efficient classes of carboxylating enzymes are enoyl-CoA carboxylases/reductases (Ecrs), which outcompete the plant enzyme RuBisCO in catalytic efficiency and fidelity by more than an order of magnitude. Here we investigated the interactions of CO2 within the active site of Ecr from Kitasatospora setae Combining experimental biochemistry, protein crystallography, and advanced computer simulations we show that 4 amino acids, N81, F170, E171, and H365, are required to create a highly efficient CO2-fixing enzyme. Together, these 4 residues anchor and position the CO2 molecule for the attack by a reactive enolate created during the catalytic cycle. Notably, a highly ordered water molecule plays an important role in an active site that is otherwise carefully shielded from water, which is detrimental to CO2 fixation. Altogether, our study reveals unprecedented molecular details of selective CO2 binding and C-C-bond formation during the catalytic cycle of nature's most efficient CO2-fixing enzyme. This knowledge provides the basis for the future development of catalytic frameworks for the capture and conversion of CO2 in biology and chemistry.
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Four amino acids define the CO2 binding pocket of enoyl-CoA carboxylases/reductases.,Stoffel GMM, Saez DA, DeMirci H, Vogeli B, Rao Y, Zarzycki J, Yoshikuni Y, Wakatsuki S, Vohringer-Martinez E, Erb TJ Proc Natl Acad Sci U S A. 2019 Jun 26. pii: 1901471116. doi:, 10.1073/pnas.1901471116. PMID:31243147<ref>PMID:31243147</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6owe" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Kitsk]]
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[[Category: Kitasatospora setae KM-6054]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: DeMirci, H]]
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[[Category: DeMirci H]]
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[[Category: Ecr]]
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[[Category: Highly efficient co2-fixing enzyme]]
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[[Category: Oxidoreductase]]
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Current revision

Enoyl-CoA carboxylases/reductases in complex with ethylmalonyl CoA

PDB ID 6owe

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OCA

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