2uz1
1.65 ANGSTROM STRUCTURE OF BENZALDEHYDE LYASE COMPLEXED WITH 2-METHYL-2,4-PENTANEDIOL
| |||||||
| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Benzoin aldolase, with EC number 4.1.2.38 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
Benzaldehyde lyase (BAL; EC 4.1.2.38) is a thiamine diphosphate (ThDP) dependent enzyme that catalyses the enantioselective carboligation of two molecules of benzaldehyde to form (R)-benzoin. BAL has hence aroused interest for its potential in the industrial synthesis of optically active benzoins and derivatives. The structure of BAL was previously solved to a resolution of 2.6 A using MAD experiments on a selenomethionine derivative [Mosbacher et al. (2005), FEBS J. 272, 6067-6076]. In this communication of parallel studies, BAL was crystallized in an alternative space group (P2(1)2(1)2(1)) and its structure refined to a resolution of 1.65 A, allowing detailed observation of the water structure, active-site interactions with ThDP and also the electron density for the co-solvent 2-methyl-2,4-pentanediol (MPD) at hydrophobic patches of the enzyme surface.
About this StructureAbout this Structure
2UZ1 is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the ThDP-dependent enzyme benzaldehyde lyase refined to 1.65 A resolution., Maraite A, Schmidt T, Ansorge-Schumacher MB, Brzozowski AM, Grogan G, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jul 1;63(Pt, 7):546-8. Epub 2007 Jun 15. PMID:17620706
Page seeded by OCA on Thu Mar 20 18:41:27 2008