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.
4rji
From Proteopedia
(Difference between revisions)
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==Acetolactate synthase from Bacillus subtilis bound to ThDP - crystal form I== | ==Acetolactate synthase from Bacillus subtilis bound to ThDP - crystal form I== | ||
| - | <StructureSection load='4rji' size='340' side='right' caption='[[4rji]], [[Resolution|resolution]] 3.20Å' scene=''> | + | <StructureSection load='4rji' size='340' side='right'caption='[[4rji]], [[Resolution|resolution]] 3.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4rji]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RJI OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4rji]] is a 4 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=4RJI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RJI 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]] 3.2Å</td></tr> |
| - | <tr id=' | + | <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=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=4rji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rji OCA], [https://pdbe.org/4rji PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rji RCSB], [https://www.ebi.ac.uk/pdbsum/4rji PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rji 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 4rji" 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]] |
| - | + | ||
Current revision
Acetolactate synthase from Bacillus subtilis bound to ThDP - crystal form I
| |||||||||||
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
