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| | <StructureSection load='6ciq' size='340' side='right'caption='[[6ciq]], [[Resolution|resolution]] 3.30Å' scene=''> | | <StructureSection load='6ciq' size='340' side='right'caption='[[6ciq]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ciq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Moota Moota]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CIQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ciq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Moorella_thermoacetica_ATCC_39073 Moorella thermoacetica ATCC 39073]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CIQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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]] 3.302Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6cin|6cin]], [[6cio|6cio]], [[6cip|6cip]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Moth_0064 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=264732 MOOTA])</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=6ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ciq OCA], [https://pdbe.org/6ciq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ciq RCSB], [https://www.ebi.ac.uk/pdbsum/6ciq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ciq ProSAT]</span></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=6ciq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ciq OCA], [http://pdbe.org/6ciq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ciq RCSB], [http://www.ebi.ac.uk/pdbsum/6ciq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ciq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q2RMD6_MOOTA Q2RMD6_MOOTA]] Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin.[PIRNR:PIRNR000159] | + | [https://www.uniprot.org/uniprot/PFOR_MOOTA PFOR_MOOTA] Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions (PubMed:10878009). The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood-Ljungdahl pathway of reductive acetogenesis. The conversion of acetyl-CoA to pyruvate links the Wood-Ljungdahl pathway of autotrophic CO2 fixation to the reductive tricarboxylic acid cycle (PubMed:10878009, PubMed:29581263). Can use methyl viologen as electron carrier in vitro (PubMed:9214293, PubMed:29581263).<ref>PMID:10878009</ref> <ref>PMID:29581263</ref> <ref>PMID:9214293</ref> <ref>PMID:10878009</ref> <ref>PMID:29581263</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Moota]] | + | [[Category: Moorella thermoacetica ATCC 39073]] |
| - | [[Category: Chen, P Y.T]] | + | [[Category: Chen PY-T]] |
| - | [[Category: Drennan, C L]] | + | [[Category: Drennan CL]] |
| - | [[Category: Coenzyme some]]
| + | |
| - | [[Category: Gated electron transfer]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Pyruvate:ferredoxin oxidoreductase]]
| + | |
| - | [[Category: Thiamine pyrophosphate]]
| + | |
| Structural highlights
Function
PFOR_MOOTA Catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism. Also catalyzes the reverse reaction, i.e. the synthesis of pyruvate from acetyl-CoA and carbon dioxide. Appears to function physiologically in both directions (PubMed:10878009). The oxidation of pyruvate by PFOR is required to connect glycolysis and the Wood-Ljungdahl pathway of reductive acetogenesis. The conversion of acetyl-CoA to pyruvate links the Wood-Ljungdahl pathway of autotrophic CO2 fixation to the reductive tricarboxylic acid cycle (PubMed:10878009, PubMed:29581263). Can use methyl viologen as electron carrier in vitro (PubMed:9214293, PubMed:29581263).[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Pyruvate:ferredoxin oxidoreductase (PFOR) is a microbial enzyme that uses thiamine pyrophosphate (TPP), three [4Fe-4S] clusters, and coenzyme A (CoA) in the reversible oxidation of pyruvate to generate acetyl-CoA and carbon dioxide. The two electrons that are generated as a result of pyruvate decarboxylation are used in the reduction of low potential ferredoxins, which provide reducing equivalents for central metabolism, including the Wood-Ljungdahl pathway. PFOR is a member of the 2-oxoacid:ferredoxin oxidoreductase (OFOR) superfamily, which plays major roles in both microbial redox reactions and carbon dioxide fixation. Here, we present a set of crystallographic snapshots of the best-studied member of this superfamily, the PFOR from Moorella thermoacetica (MtPFOR). These snapshots include the native structure, those of lactyl-TPP and acetyl-TPP reaction intermediates, and the first of an OFOR with CoA bound. These structural data reveal the binding site of CoA as domain III, the function of which in OFORs was previously unknown, and establish sequence motifs for CoA binding in the OFOR superfamily. MtPFOR structures further show that domain III undergoes a conformational change upon CoA binding that seals off the active site and positions the thiolate of CoA directly adjacent to the TPP cofactor. These structural findings provide a molecular basis for the experimental observation that CoA binding accelerates catalysis by 10(5)-fold.
Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica.,Chen PY, Aman H, Can M, Ragsdale SW, Drennan CL Proc Natl Acad Sci U S A. 2018 Mar 26. pii: 1722329115. doi:, 10.1073/pnas.1722329115. PMID:29581263[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Furdui C, Ragsdale SW. The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway. J Biol Chem. 2000 Sep 15;275(37):28494-9. PMID:10878009 doi:http://dx.doi.org/10.1074/jbc.M003291200
- ↑ Chen PY, Aman H, Can M, Ragsdale SW, Drennan CL. Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica. Proc Natl Acad Sci U S A. 2018 Mar 26. pii: 1722329115. doi:, 10.1073/pnas.1722329115. PMID:29581263 doi:http://dx.doi.org/10.1073/pnas.1722329115
- ↑ Menon S, Ragsdale SW. Mechanism of the Clostridium thermoaceticum pyruvate:ferredoxin oxidoreductase: evidence for the common catalytic intermediacy of the hydroxyethylthiamine pyropyrosphate radical. Biochemistry. 1997 Jul 15;36(28):8484-94. PMID:9214293 doi:10.1021/bi970403k
- ↑ Furdui C, Ragsdale SW. The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway. J Biol Chem. 2000 Sep 15;275(37):28494-9. PMID:10878009 doi:http://dx.doi.org/10.1074/jbc.M003291200
- ↑ Chen PY, Aman H, Can M, Ragsdale SW, Drennan CL. Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica. Proc Natl Acad Sci U S A. 2018 Mar 26. pii: 1722329115. doi:, 10.1073/pnas.1722329115. PMID:29581263 doi:http://dx.doi.org/10.1073/pnas.1722329115
- ↑ Chen PY, Aman H, Can M, Ragsdale SW, Drennan CL. Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica. Proc Natl Acad Sci U S A. 2018 Mar 26. pii: 1722329115. doi:, 10.1073/pnas.1722329115. PMID:29581263 doi:http://dx.doi.org/10.1073/pnas.1722329115
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