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2v3w

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Revision as of 07:25, 17 January 2018

Crystal structure of the benzoylformate decarboxylase variant L461A from Pseudomonas putida

Structural highlights

2v3w is a 4 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1bfd, 1mcz, 1pi3, 1po7, 1q6z, 1yno
Activity:	Benzoylformate decarboxylase, with EC number 4.1.1.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v3w"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the benzoylformate decarboxylase variant L461A from Pseudomonas putida==
 <StructureSection load='2v3w' size='340' side='right' caption='[[2v3w]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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='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'>[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]</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>
 == Evolutionary Conservation ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v3/2v3w_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v3/2v3w_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 44: / Line 45: @@
 [[Category: Walter, L]]
 [[Category: Aromatic hydrocarbons catabolism]]
+[[Category: Calcium]]
 [[Category: Carboligation]]
 [[Category: Decarboxylase]]

2v3w

From Proteopedia

Revision as of 07:25, 17 January 2018

Crystal structure of the benzoylformate decarboxylase variant L461A from Pseudomonas putida

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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