2ag1

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[[Image:2ag1.gif|left|200px]]
[[Image:2ag1.gif|left|200px]]
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{{Structure
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|PDB= 2ag1 |SIZE=350|CAPTION= <scene name='initialview01'>2ag1</scene>, resolution 2.58&Aring;
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The line below this paragraph, containing "STRUCTURE_2ag1", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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|GENE=
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{{STRUCTURE_2ag1| PDB=2ag1 | SCENE= }}
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|RELATEDENTRY=[[2ag0|2AG0]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ag1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ag1 OCA], [http://www.ebi.ac.uk/pdbsum/2ag1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ag1 RCSB]</span>
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'''Crystal structure of Benzaldehyde lyase (BAL)- SeMet'''
'''Crystal structure of Benzaldehyde lyase (BAL)- SeMet'''
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[[Category: Mueller, M.]]
[[Category: Mueller, M.]]
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
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[[Category: tetramer]]
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[[Category: Tetramer]]
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[[Category: thdp dependent fold]]
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[[Category: Thdp dependent fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:00:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:52:14 2008''
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Revision as of 16:00, 3 May 2008

Image:2ag1.gif

Template:STRUCTURE 2ag1

Crystal structure of Benzaldehyde lyase (BAL)- SeMet


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 Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from 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:16302970 Page seeded by OCA on Sat May 3 19:00:30 2008

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