2uz1: Difference between revisions
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==Overview== | ==Overview== | ||
Benzaldehyde lyase (BAL; EC 4.1.2.38) is a thiamine diphosphate (ThDP) | 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 Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
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 | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17620706 17620706] | ||
[[Category: Benzoin aldolase]] | [[Category: Benzoin aldolase]] | ||
[[Category: Pseudomonas fluorescens]] | [[Category: Pseudomonas fluorescens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ansorge-Schumacher, M | [[Category: Ansorge-Schumacher, M B.]] | ||
[[Category: Brzozowski, A | [[Category: Brzozowski, A M.]] | ||
[[Category: Grogan, G.]] | [[Category: Grogan, G.]] | ||
[[Category: Maraite, A.]] | [[Category: Maraite, A.]] | ||
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[[Category: thiamine pyrophosphate]] | [[Category: thiamine pyrophosphate]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:51:42 2008'' | ||
Revision as of 19:51, 21 February 2008
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1.65 ANGSTROM STRUCTURE OF BENZALDEHYDE LYASE COMPLEXED WITH 2-METHYL-2,4-PENTANEDIOL
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 with and as ligands. Active as Benzoin aldolase, with EC number 4.1.2.38 Known structural/functional Site: . 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
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