6ciq: Difference between revisions
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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. 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 [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> | ||
</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='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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[d_1000232405|d_1000232405]], [[d_1000232406|d_1000232406]], [[d_1000232407|d_1000232407]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[d_1000232405|d_1000232405]], [[d_1000232406|d_1000232406]], [[d_1000232407|d_1000232407]]</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'>[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> | <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] | [[http://www.uniprot.org/uniprot/Q2RMD6_MOOTA Q2RMD6_MOOTA]] Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin.[PIRNR:PIRNR000159] | ||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:29581263</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ciq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Moota]] | |||
[[Category: Chen, P Y.T]] | [[Category: Chen, P Y.T]] | ||
[[Category: Drennan, C L]] | [[Category: Drennan, C L]] | ||
Revision as of 17:20, 11 April 2018
Pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica with coenzyme A boundPyruvate:ferredoxin oxidoreductase from Moorella thermoacetica with coenzyme A bound
Structural highlights
Function[Q2RMD6_MOOTA] Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin.[PIRNR:PIRNR000159] Publication Abstract from PubMedPyruvate: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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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