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2uz1
From Proteopedia
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|PDB= 2uz1 |SIZE=350|CAPTION= <scene name='initialview01'>2uz1</scene>, resolution 1.65Å | |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> | |SITE= <scene name='pdbsite=AC1:Mpd+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uz1 OCA], [http://www.ebi.ac.uk/pdbsum/2uz1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2uz1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Maraite, A.]] | [[Category: Maraite, A.]] | ||
[[Category: Schmidt, T.]] | [[Category: Schmidt, T.]] | ||
| - | [[Category: MPD]] | ||
| - | [[Category: TPP]] | ||
[[Category: benzaldehyde]] | [[Category: benzaldehyde]] | ||
[[Category: benzoin]] | [[Category: benzoin]] | ||
| Line 37: | Line 38: | ||
[[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 Mon Mar 31 05:06:29 2008'' |
Revision as of 02:06, 31 March 2008
| |||||||
| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Benzoin aldolase, with EC number 4.1.2.38 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
1.65 ANGSTROM STRUCTURE OF BENZALDEHYDE LYASE COMPLEXED WITH 2-METHYL-2,4-PENTANEDIOL
Overview
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
2UZ1 is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.
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:17620706
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