2j5i
From Proteopedia
(New page: 200px<br /><applet load="2j5i" size="350" color="white" frame="true" align="right" spinBox="true" caption="2j5i, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...) |
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==Overview== | ==Overview== | ||
| - | The crystal structure of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) from | + | 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== | ==About this Structure== | ||
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[[Category: Pseudomonas fluorescens]] | [[Category: Pseudomonas fluorescens]] | ||
[[Category: Trans-feruloyl-CoA hydratase]] | [[Category: Trans-feruloyl-CoA hydratase]] | ||
| - | [[Category: Brzozowski, A | + | [[Category: Brzozowski, A M.]] |
[[Category: Grogan, G.]] | [[Category: Grogan, G.]] | ||
[[Category: Lebedev, A.]] | [[Category: Lebedev, A.]] | ||
| - | [[Category: Leonard, P | + | [[Category: Leonard, P M.]] |
| - | [[Category: Marshall, C | + | [[Category: Marshall, C M.]] |
| - | [[Category: Smith, D | + | [[Category: Smith, D J.]] |
| - | [[Category: Verma, C | + | [[Category: Verma, C S.]] |
| - | [[Category: Walton, N | + | [[Category: Walton, N J.]] |
[[Category: aldolase]] | [[Category: aldolase]] | ||
[[Category: coenzyme-a]] | [[Category: coenzyme-a]] | ||
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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 Thu Feb 21 17:59:24 2008'' |
Revision as of 15:59, 21 February 2008
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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. Active as Trans-feruloyl-CoA hydratase, with EC number 4.2.1.101 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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