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4mq5

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==Crystal Structure of Benzoylformate Decarboxylase Mutant A306F==
==Crystal Structure of Benzoylformate Decarboxylase Mutant A306F==
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<StructureSection load='4mq5' size='340' side='right' caption='[[4mq5]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='4mq5' size='340' side='right'caption='[[4mq5]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4mq5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MQ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MQ5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4mq5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MQ5 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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]] 1.502&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mpp|4mpp]], [[4mpr|4mpr]]</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Benzoylformate_decarboxylase Benzoylformate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.7 4.1.1.7] </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=4mq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mq5 OCA], [https://pdbe.org/4mq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mq5 RCSB], [https://www.ebi.ac.uk/pdbsum/4mq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mq5 ProSAT]</span></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=4mq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mq5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mq5 RCSB], [http://www.ebi.ac.uk/pdbsum/4mq5 PDBsum]</span></td></tr>
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</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/MDLC_PSEPU MDLC_PSEPU]
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The X-ray structure of benzoylformate decarboxylase (BFDC) from Pseudomonas putida ATCC 12633 shows it to be a tetramer. This was believed to be typical of all thiamin diphosphate-dependent decarboxylases until recently when the structure of KdcA, a branched-chain 2-keto acid decarboxylase from Lactococcus lactis, showed it to be a homodimer. This lent credence to earlier unfolding experiments on pyruvate decarboxylase from Saccharomyces cerevisiae that indicated that it might be active as a dimer. To investigate this possibility in BFDC, we sought to shift the equilibrium toward dimer formation. Point mutations were made in the noncatalytic monomer-monomer interfaces, but these had a minimal effect on both tetramer formation and catalytic activity. Subsequently, the R141E/Y288A/A306F variant was shown by analytical ultracentrifugation to be partially dimeric. It was also found to be catalytically inactive. Further experiments revealed that just two mutations, R141E and A306F, were sufficient to markedly alter the dimer-tetramer equilibrium and to provide an ~450-fold decrease in kcat. Equilibrium denaturation studies suggested that the residual activity was possibly due to the presence of residual tetramer. The structures of the R141E and A306F variants, determined to &lt;1.5 A resolution, hinted that disruption of the monomer interfaces will be accompanied by movement of a loop containing Leu109 and Leu110. As these residues contribute to the hydrophobicity of the active site and the correct positioning of the substrate, it seems that tetramer formation may well be critical to the catalytic activity of BFDC.
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Perturbation of the monomer-monomer interfaces of the benzoylformate decarboxylase tetramer.,Andrews FH, Rogers MP, Paul LN, McLeish MJ Biochemistry. 2014 Jul 15;53(27):4358-67. doi: 10.1021/bi500081r. Epub 2014 Jul, 3. PMID:24956165<ref>PMID:24956165</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Benzoylformate decarboxylase]]
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[[Category: Large Structures]]
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[[Category: Andrews, F H]]
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[[Category: Pseudomonas putida]]
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[[Category: McLeish, M J]]
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[[Category: Andrews FH]]
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[[Category: Cytol]]
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[[Category: McLeish MJ]]
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[[Category: Lyase]]
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[[Category: Thdp-dependent]]
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Current revision

Crystal Structure of Benzoylformate Decarboxylase Mutant A306F

PDB ID 4mq5

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