View source for 2ag1

[[Image:2ag1.gif|left|200px]]<br /><applet load="2ag1" size="350" color="white" frame="true" align="right" spinBox="true" 
caption="2ag1, resolution 2.58&Aring;" />
'''Crystal structure of Benzaldehyde lyase (BAL)- SeMet'''<br />

==Overview==
Pseudomonas fluorescens is able to grow on R-benzoin as the sole carbon, and energy source because it harbours the enzyme benzaldehyde lyase that, cleaves the acyloin linkage using thiamine diphosphate (ThDP) as a, cofactor. In the reverse reaction, this lyase catalyses the carboligation, of two aldehydes with high substrate and stereospecificity. The enzyme, structure was determined by X-ray diffraction at 2.6 A resolution. A, structure-based comparison with other proteins showed that benzaldehyde, lyase belongs to a group of closely related ThDP-dependent enzymes. The, ThDP cofactors of these enzymes are fixed at their two ends in separate, domains, suspending a comparatively mobile thiazolium ring between them., While the residues binding the two ends of ThDP are well conserved, the, lining of the active centre pocket around the thiazolium moiety varies, greatly within the group. Accounting for the known reaction chemistry, the, natural substrate R-benzoin was modelled unambiguously into the active, centre of the reported benzaldehyde lyase. Due to its substrate spectrum, and stereospecificity, the enzyme extends the synthetic potential for, carboligations appreciably.

==About this Structure==
2AG1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=TPP:'>TPP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AG1 OCA]. 

==Reference==
Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens., Mosbacher TG, Mueller M, Schulz GE, FEBS J. 2005 Dec;272(23):6067-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16302970 16302970]
[[Category: Benzoin aldolase]]
[[Category: Pseudomonas fluorescens]]
[[Category: Single protein]]
[[Category: Mosbacher, T.G.]]
[[Category: Mueller, M.]]
[[Category: Schulz, G.E.]]
[[Category: MG]]
[[Category: TPP]]
[[Category: tetramer]]
[[Category: thdp dependent fold]]

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