4rjk: Difference between revisions
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==Acetolactate synthase from Bacillus subtilis bound to LThDP - crystal form II== | ==Acetolactate synthase from Bacillus subtilis bound to LThDP - crystal form II== | ||
<StructureSection load='4rjk' size='340' side='right' caption='[[4rjk]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4rjk' size='340' side='right'caption='[[4rjk]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4rjk]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RJK OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4rjk]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_PY79 Bacillus subtilis PY79]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RJK 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=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>, <scene name='pdbligand=TDL:3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-2-(1-CARBOXY-1-HYDROXYETHYL)-5-(2-{[HYDROXY(PHOSPHONOOXY)PHOSPHORYL]OXY}ETHYL)-4-METHYL-1,3-THIAZOL-3-IUM'>TDL</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene>, <scene name='pdbligand=TDL:3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-2-(1-CARBOXY-1-HYDROXYETHYL)-5-(2-{[HYDROXY(PHOSPHONOOXY)PHOSPHORYL]OXY}ETHYL)-4-METHYL-1,3-THIAZOL-3-IUM'>TDL</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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=4rjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rjk OCA], [https://pdbe.org/4rjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rjk RCSB], [https://www.ebi.ac.uk/pdbsum/4rjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rjk ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Isobutanol is deemed to be a next-generation biofuel and a renewable platform chemical.1 Non-natural biosynthetic pathways for isobutanol production have been implemented in cell-based and in vitro systems with Bacillus subtilis acetolactate synthase (AlsS) as key biocatalyst.2-6 AlsS catalyzes the condensation of two pyruvate molecules to acetolactate with thiamine diphosphate and Mg2+ as cofactors. AlsS also catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol. Our phylogenetic analysis suggests that the ALS enzyme family forms a distinct subgroup of ThDP-dependent enzymes. To unravel catalytically relevant structure-function relationships, we solved the AlsS crystal structure at 2.3 A in the presence of ThDP, Mg2+ and in a transition state with a 2-lactyl moiety bound to ThDP. We supplemented our structural data by point mutations in the active site to identify catalytically important residues. | |||
Detailed Structure-Function Correlations of Bacillus subtilis Acetolactate Synthase.,Sommer B, von Moeller H, Haack M, Qoura F, Langner C, Bourenkov G, Garbe D, Loll B, Bruck T Chembiochem. 2014 Nov 13. doi: 10.1002/cbic.201402541. PMID:25393087<ref>PMID:25393087</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4rjk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus subtilis PY79]] | ||
[[Category: Bourenkov | [[Category: Large Structures]] | ||
[[Category: Brueck | [[Category: Bourenkov G]] | ||
[[Category: Garbe | [[Category: Brueck T]] | ||
[[Category: Haack | [[Category: Garbe D]] | ||
[[Category: Langner | [[Category: Haack M]] | ||
[[Category: Loll | [[Category: Langner C]] | ||
[[Category: Loll B]] | |||
[[Category: Qoura | [[Category: Qoura F]] | ||
[[Category: Sommer | [[Category: Sommer B]] | ||
[[Category: | [[Category: Von Moeller H]] | ||
Latest revision as of 09:21, 15 November 2023
Acetolactate synthase from Bacillus subtilis bound to LThDP - crystal form II
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