2ag1: Difference between revisions
New page: left|200px<br /><applet load="2ag1" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ag1, resolution 2.58Å" /> '''Crystal structure of... |
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==Overview== | ==Overview== | ||
Pseudomonas fluorescens is able to grow on R-benzoin as the sole carbon | 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== | ==About this Structure== | ||
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[[Category: Pseudomonas fluorescens]] | [[Category: Pseudomonas fluorescens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Mosbacher, T | [[Category: Mosbacher, T G.]] | ||
[[Category: Mueller, M.]] | [[Category: Mueller, M.]] | ||
[[Category: Schulz, G | [[Category: Schulz, G E.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
[[Category: TPP]] | [[Category: TPP]] | ||
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[[Category: thdp dependent fold]] | [[Category: thdp dependent fold]] | ||
''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 16:27:02 2008'' | ||
Revision as of 17:27, 21 February 2008
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Crystal structure of Benzaldehyde lyase (BAL)- SeMet
OverviewOverview
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 StructureAbout this Structure
2AG1 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 Full crystallographic information is available from OCA.
ReferenceReference
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
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