2j5i
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Trans-feruloyl-CoA_hydratase Trans-feruloyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.101 4.2.1.101] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trans-feruloyl-CoA_hydratase Trans-feruloyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.101 4.2.1.101] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j5i OCA], [http://www.ebi.ac.uk/pdbsum/2j5i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j5i RCSB]</span> | ||
}} | }} | ||
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[[Category: vanillin]] | [[Category: vanillin]] | ||
| - | ''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 03:53:15 2008'' |
Revision as of 00:53, 31 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Trans-feruloyl-CoA hydratase, with EC number 4.2.1.101 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE
Overview
The crystal structure of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) from Pseudomonas fluorescens AN103 has been solved to 1.8 A resolution. HCHL is a member of the crotonase superfamily and catalyses the hydration of the acyl-CoA thioester of ferulic acid [3-(4-hydroxy-3-methoxy-phenyl)prop-2-enoic acid] and the subsequent retro-aldol cleavage of the hydrated intermediate to yield vanillin (4-hydroxy-3-methoxy-benzaldehyde). The structure contains 12 molecules in the asymmetric unit, in which HCHL assumes a hexameric structure of two stacked trimers. The substrate, feruloyl-CoA, was modelled into the active site based on the structure of enoyl-CoA hydratase bound to the feruloyl-CoA-like substrate 4-(N,N-dimethylamino)-cinnamoyl-CoA (PDB code 1ey3). Feruloyl-CoA was bound in this model between helix 3 of the A subunit and helix 9 of the B subunit. A highly ordered structural water in the HCHL structure coincided with the thioester carbonyl of feruloyl-CoA in the model, suggesting that the oxyanion hole for stabilization of a thioester-derived enolate, characteristic of coenzyme-A dependent members of the crotonase superfamily, is conserved. The model also suggested that a strong hydrogen bond between the phenolic hydroxyl groups of feruloyl-CoA and BTyr239 may be an important determinant of the enzyme's ability to discriminate between the natural substrate and cinnamoyl-CoA, which is not a substrate.
About this Structure
2J5I is a Protein complex structure of sequences from Pseudomonas fluorescens. Full crystallographic information is available from OCA.
Reference
The 1.8 A resolution structure of hydroxycinnamoyl-coenzyme A hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that catalyses the transformation of feruloyl-coenzyme A to vanillin., Leonard PM, Brzozowski AM, Lebedev A, Marshall CM, Smith DJ, Verma CS, Walton NJ, Grogan G, Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1494-501. Epub, 2006 Nov 23. PMID:17139085
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