2uz1 | pdb_00002uz1

1.65 Angstrom structure of Benzaldehyde Lyase complexed with 2-methyl- 2,4-pentanediol

spinqualitylabelsall models 2uz1, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2uz1 is a 4 chain structure with sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: MPD, TPP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9F4L3_PSEFL Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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