This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4rjk
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4rjk is ON HOLD Authors: Sommer, B., von Moeller, H., Haack, M., Qoura, F., Langner, C., Bourenkov, G., Garbe, D., Brueck, T., Loll, B. Description...) |
|||
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <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='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> | ||
| + | </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__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus subtilis PY79]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bourenkov G]] | ||
| + | [[Category: Brueck T]] | ||
| + | [[Category: Garbe D]] | ||
| + | [[Category: Haack M]] | ||
| + | [[Category: Langner C]] | ||
| + | [[Category: Loll B]] | ||
| + | [[Category: Qoura F]] | ||
| + | [[Category: Sommer B]] | ||
| + | [[Category: Von Moeller H]] | ||
Current revision
Acetolactate synthase from Bacillus subtilis bound to LThDP - crystal form II
| |||||||||||
Categories: Bacillus subtilis PY79 | Large Structures | Bourenkov G | Brueck T | Garbe D | Haack M | Langner C | Loll B | Qoura F | Sommer B | Von Moeller H
