2UZ1
1.65 Angstrom structure of Benzaldehyde Lyase complexed with 2-methyl- 2,4-pentanediol
Summary for 2UZ1
| Entry DOI | 10.2210/pdb2uz1/pdb |
| Related | 2AG0 2AG1 |
| Descriptor | BENZALDEHYDE LYASE, THIAMINE DIPHOSPHATE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (5 entities in total) |
| Functional Keywords | thiamine diphosphate, thiamine pyrophosphate, lyase, benzoin, flavoprotein, benzaldehyde |
| Biological source | PSEUDOMONAS FLUORESCENS More |
| Total number of polymer chains | 4 |
| Total formula weight | 237960.20 |
| Authors | Maraite, A.,Schmidt, T.,Ansorge-Schumacher, M.B.,Brzozowski, A.M.,Grogan, G. (deposition date: 2007-04-23, release date: 2007-07-24, Last modification date: 2023-12-13) |
| Primary citation | Maraite, A.,Schmidt, T.,Ansorge-Schumacher, M.B.,Brzozowski, A.M.,Grogan, G. Structure of the Thdp-Dependent Enzyme Benzaldehyde Lyase Refined to 1.65 A Resolution. Acta Crystallogr.,Sect.F, 63:546-, 2007 Cited by PubMed Abstract: 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. PubMed: 17620706DOI: 10.1107/S1744309107028576 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
Download full validation report
