4RJK

Acetolactate synthase from Bacillus subtilis bound to LThDP - crystal form II

Summary for 4RJK

• Entry DOI: 10.2210/pdb4rjk/pdb
• Related: 1OZF 1OZG 1OZH 4RJI 4RJJ
• Descriptor: Acetolactate synthase, THIAMINE DIPHOSPHATE, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: lyase, thdp
• Biological source: Bacillus subtilis
• Total number of polymer chains: 8
• Total formula weight: 509776.82

Authors

Sommer, B.,von Moeller, H.,Haack, M.,Qoura, F.,Langner, C.,Bourenkov, G.,Garbe, D.,Brueck, T.,Loll, B. (deposition date: 2014-10-09, release date: 2014-10-22, Last modification date: 2023-11-15)

Primary citation

Sommer, B.,von Moeller, H.,Haack, M.,Qoura, F.,Langner, C.,Bourenkov, G.,Garbe, D.,Loll, B.,Bruck, T.
Detailed Structure-Function Correlations of Bacillus subtilis Acetolactate Synthase.
Chembiochem, 16:110-118, 2015

PubMed Abstract: 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 Mg(2+) 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 Å in the presence of ThDP, Mg(2+) 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.

PubMed: 25393087
DOI: 10.1002/cbic.201402541

Experimental method

X-RAY DIFFRACTION (2.5 Å)