2uz1: Difference between revisions
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[[Image:2uz1.gif|left|200px]] | [[Image:2uz1.gif|left|200px]] | ||
'''1.65 ANGSTROM STRUCTURE OF BENZALDEHYDE LYASE COMPLEXED WITH 2-METHYL-2,4-PENTANEDIOL''' | {{Structure | ||
|PDB= 2uz1 |SIZE=350|CAPTION= <scene name='initialview01'>2uz1</scene>, resolution 1.65Å | |||
|SITE= <scene name='pdbsite=AC1:Mpd+Binding+Site+For+Chain+B'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Benzoin_aldolase Benzoin aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.38 4.1.2.38] | |||
|GENE= | |||
}} | |||
'''1.65 ANGSTROM STRUCTURE OF BENZALDEHYDE LYASE COMPLEXED WITH 2-METHYL-2,4-PENTANEDIOL''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2UZ1 is a [ | 2UZ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UZ1 OCA]. | ||
==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 Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jul 1;63(Pt, 7):546-8. Epub 2007 Jun 15. PMID:[http:// | 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://www.ncbi.nlm.nih.gov/pubmed/17620706 17620706] | ||
[[Category: Benzoin aldolase]] | [[Category: Benzoin aldolase]] | ||
[[Category: Pseudomonas fluorescens]] | [[Category: Pseudomonas fluorescens]] | ||
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[[Category: thiamine pyrophosphate]] | [[Category: thiamine pyrophosphate]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:41:27 2008'' | ||
Revision as of 19:41, 20 March 2008
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| , resolution 1.65Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Benzoin aldolase, with EC number 4.1.2.38 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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