4bt6: Difference between revisions
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==acetolactate decarboxylase with a bound glycerol== | ==acetolactate decarboxylase with a bound glycerol== | ||
<StructureSection load='4bt6' size='340' side='right' caption='[[4bt6]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4bt6' size='340' side='right'caption='[[4bt6]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4bt6]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4bt6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BT6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4bt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bt6 OCA], [https://pdbe.org/4bt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bt6 RCSB], [https://www.ebi.ac.uk/pdbsum/4bt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bt6 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ALDC_BREBE ALDC_BREBE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Brevibacillus brevis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: A Marlow V]] | ||
[[Category: | [[Category: Fulop V]] | ||
[[Category: Najmudin | [[Category: Najmudin S]] | ||
[[Category: Rea | [[Category: Rea D]] | ||
[[Category: Wills | [[Category: Wills M]] | ||
Latest revision as of 14:57, 20 December 2023
acetolactate decarboxylase with a bound glycerolacetolactate decarboxylase with a bound glycerol
Structural highlights
FunctionPublication Abstract from PubMedAcetolactate decarboxylase catalyzes the conversion of both enantiomers of acetolactate to the (R)-enantiomer of acetoin, via a mechanism that has been shown to involve a prior rearrangement of the non-natural (R)-enantiomer substrate to the natural (S)-enantiomer. In this paper, a series of crystal structures of ALDC complex with designed transition state mimics are reported. These structures, coupled with inhibition studies and site-directed mutagenesis provide an improved understanding of the molecular processes involved in the stereoselective decarboxylation/protonation events. A mechanism for the transformation of each enantiomer of acetolactate is proposed. Structure and Mechanism of Acetolactate Decarboxylase.,Marlow VA, Rea D, Najmudin S, Wills M, Fulop V ACS Chem Biol. 2013 Aug 28. PMID:23985082[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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