4c3s: Difference between revisions
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==Structure of a propionaldehyde dehydrogenase from the Clostridium phytofermentans fucose utilisation bacterial microcompartment== | ==Structure of a propionaldehyde dehydrogenase from the Clostridium phytofermentans fucose utilisation bacterial microcompartment== | ||
<StructureSection load='4c3s' size='340' side='right' caption='[[4c3s]], [[Resolution|resolution]] 1.64Å' scene=''> | <StructureSection load='4c3s' size='340' side='right' caption='[[4c3s]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c3s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4c3s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700394 Atcc 700394]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3S FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetaldehyde_dehydrogenase_(acetylating) Acetaldehyde dehydrogenase (acetylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.10 1.2.1.10] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetaldehyde_dehydrogenase_(acetylating) Acetaldehyde dehydrogenase (acetylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.10 1.2.1.10] </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=4c3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3s RCSB], [http://www.ebi.ac.uk/pdbsum/4c3s PDBsum]</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=4c3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3s OCA], [http://pdbe.org/4c3s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c3s RCSB], [http://www.ebi.ac.uk/pdbsum/4c3s PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The breakdown of fucose and rhamnose released from plant cell walls by the cellulolytic soil bacterium Clostridium phytofermentans produces toxic aldehyde intermediates. To enable growth on these carbon sources, the pathway for the breakdown of fucose and rhamnose is encapsulated within a bacterial microcompartment (BMC). These proteinaceous organelles sequester the toxic aldehyde intermediates and allow the efficient action of acylating aldehyde dehydrogenase enzymes to produce an acyl-CoA that is ultimately used in substrate-level phosphorylation to produce ATP. Here we analyse the kinetics of the aldehyde dehydrogenase enzyme from the fucose/rhamnose utilisation BMC with different short-chain fatty aldehydes and show that it has activity against substrates with up to six carbon atoms, with optimal activity against propionaldehyde. We have also determined the X-ray crystal structure of this enzyme in complex with CoA and show that the adenine nucleotide of this cofactor is bound in a distinct pocket to the same group in NAD(+). This work is the first report of the structure of CoA bound to an aldehyde dehydrogenase enzyme and our crystallographic model provides important insight into the differences within the active site that distinguish the acylating from non-acylating aldehyde dehydrogenase enzymes. | |||
Insight into Coenzyme A cofactor binding and the mechanism of acyl-transfer in an acylating aldehyde dehydrogenase from Clostridium phytofermentans.,Tuck LR, Altenbach K, Ang TF, Crawshaw AD, Campopiano DJ, Clarke DJ, Marles-Wright J Sci Rep. 2016 Feb 22;6:22108. doi: 10.1038/srep22108. PMID:26899032<ref>PMID:26899032</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4c3s" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Aldehyde dehydrogenase|Aldehyde dehydrogenase]] | *[[Aldehyde dehydrogenase|Aldehyde dehydrogenase]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 700394]] | ||
[[Category: Altenbach, K]] | [[Category: Altenbach, K]] | ||
[[Category: Ang, T F]] | [[Category: Ang, T F]] | ||
Revision as of 19:31, 10 May 2016
Structure of a propionaldehyde dehydrogenase from the Clostridium phytofermentans fucose utilisation bacterial microcompartmentStructure of a propionaldehyde dehydrogenase from the Clostridium phytofermentans fucose utilisation bacterial microcompartment
Structural highlights
Publication Abstract from PubMedThe breakdown of fucose and rhamnose released from plant cell walls by the cellulolytic soil bacterium Clostridium phytofermentans produces toxic aldehyde intermediates. To enable growth on these carbon sources, the pathway for the breakdown of fucose and rhamnose is encapsulated within a bacterial microcompartment (BMC). These proteinaceous organelles sequester the toxic aldehyde intermediates and allow the efficient action of acylating aldehyde dehydrogenase enzymes to produce an acyl-CoA that is ultimately used in substrate-level phosphorylation to produce ATP. Here we analyse the kinetics of the aldehyde dehydrogenase enzyme from the fucose/rhamnose utilisation BMC with different short-chain fatty aldehydes and show that it has activity against substrates with up to six carbon atoms, with optimal activity against propionaldehyde. We have also determined the X-ray crystal structure of this enzyme in complex with CoA and show that the adenine nucleotide of this cofactor is bound in a distinct pocket to the same group in NAD(+). This work is the first report of the structure of CoA bound to an aldehyde dehydrogenase enzyme and our crystallographic model provides important insight into the differences within the active site that distinguish the acylating from non-acylating aldehyde dehydrogenase enzymes. Insight into Coenzyme A cofactor binding and the mechanism of acyl-transfer in an acylating aldehyde dehydrogenase from Clostridium phytofermentans.,Tuck LR, Altenbach K, Ang TF, Crawshaw AD, Campopiano DJ, Clarke DJ, Marles-Wright J Sci Rep. 2016 Feb 22;6:22108. doi: 10.1038/srep22108. PMID:26899032[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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