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| | <StructureSection load='2v3w' size='340' side='right'caption='[[2v3w]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2v3w' size='340' side='right'caption='[[2v3w]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2v3w]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V3W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2v3w]] is a 4 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=2V3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V3W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bfd|1bfd]], [[1mcz|1mcz]], [[1pi3|1pi3]], [[1po7|1po7]], [[1q6z|1q6z]], [[1yno|1yno]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr> |
| - | <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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3w OCA], [https://pdbe.org/2v3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v3w RCSB], [https://www.ebi.ac.uk/pdbsum/2v3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v3w 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=2v3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3w OCA], [http://pdbe.org/2v3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v3w RCSB], [http://www.ebi.ac.uk/pdbsum/2v3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v3w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MDLC_PSEPU MDLC_PSEPU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fluorescens putidus flugge 1886]] | |
| - | [[Category: Benzoylformate decarboxylase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Berthold, C L]] | + | [[Category: Pseudomonas putida]] |
| - | [[Category: Gauchenova, K]] | + | [[Category: Berthold CL]] |
| - | [[Category: Gocke, D]] | + | [[Category: Gauchenova K]] |
| - | [[Category: Knoll, M]] | + | [[Category: Gocke D]] |
| - | [[Category: Kolter, G]] | + | [[Category: Knoll M]] |
| - | [[Category: Mueller, M]] | + | [[Category: Kolter G]] |
| - | [[Category: Pleiss, J]] | + | [[Category: Mueller M]] |
| - | [[Category: Pohl, M]] | + | [[Category: Pleiss J]] |
| - | [[Category: Schneider, G]] | + | [[Category: Pohl M]] |
| - | [[Category: Walter, L]] | + | [[Category: Schneider G]] |
| - | [[Category: Aromatic hydrocarbons catabolism]]
| + | [[Category: Walter L]] |
| - | [[Category: Calcium]]
| + | |
| - | [[Category: Carboligation]]
| + | |
| - | [[Category: Decarboxylase]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Magnesium]]
| + | |
| - | [[Category: Mandelate pathway]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Rational protein design]]
| + | |
| - | [[Category: Thdp-dependent]]
| + | |
| - | [[Category: Thiamine pyrophosphate]]
| + | |
| Structural highlights
Function
MDLC_PSEPU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Benzoylformate decarboxylase (BFD) from Pseudomonas putida is an exceptional thiamin diphosphate-dependent enzyme, as it catalyzes the formation of (S)-2-hydroxy-1-phenylpropan-1-one from benzaldehyde and acetaldehyde. This is the only currently known S-selective reaction (92 % ee) catalyzed by this otherwise R-selective class of enzymes. Here we describe the molecular basis of the introduction of S selectivity into ThDP-dependent decarboxylases. By shaping the active site of BFD through the use of rational protein design, structural analysis, and molecular modeling, optimal steric stabilization of the acceptor aldehyde in a structural element called the S pocket was identified as the predominant interaction for adjusting stereoselectivity. Our studies revealed Leu461 as a hot spot for stereoselectivity in BFD. Exchange to alanine and glycine resulted in variants that catalyze the S-stereoselective addition of larger acceptor aldehydes, such as propanal with benzaldehyde and its derivatives-a reaction not catalyzed by the wild-type enzyme. Crystal structure analysis of the variant BFDL461A supports the modeling studies.
Rational protein design of ThDP-dependent enzymes-engineering stereoselectivity.,Gocke D, Walter L, Gauchenova E, Kolter G, Knoll M, Berthold CL, Schneider G, Pleiss J, Muller M, Pohl M Chembiochem. 2008 Feb 15;9(3):406-12. PMID:18224647[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gocke D, Walter L, Gauchenova E, Kolter G, Knoll M, Berthold CL, Schneider G, Pleiss J, Muller M, Pohl M. Rational protein design of ThDP-dependent enzymes-engineering stereoselectivity. Chembiochem. 2008 Feb 15;9(3):406-12. PMID:18224647 doi:http://dx.doi.org/10.1002/cbic.200700598
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