4rjj

<StructureSection load='4rjj' size='340' side='right' caption='[[4rjj]], [[Resolution|resolution]] 2.34&Aring;' scene=''>

<table><tr><td colspan='2'>[[4rjj]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RJJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RJJ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lyase Lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.18 4.1.3.18] </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=4rjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rjj OCA], [http://pdbe.org/4rjj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rjj RCSB], [http://www.ebi.ac.uk/pdbsum/4rjj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rjj ProSAT]</span></td></tr>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 4rjj" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Lyase]]

[[Category: Bourenkov, G]]

[[Category: Brueck, T]]

[[Category: Garbe, D]]

[[Category: Haack, M]]

[[Category: Langner, C]]

[[Category: Loll, B]]

[[Category: Moeller, H von]]

[[Category: Qoura, F]]

[[Category: Sommer, B]]

[[Category: Thdp]]