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2j5i

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[[Image:2j5i.gif|left|200px]]<br /><applet load="2j5i" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2j5i.gif|left|200px]]
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caption="2j5i, resolution 1.80&Aring;" />
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'''CRYSTAL STRUCTURE OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE'''<br />
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{{Structure
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|PDB= 2j5i |SIZE=350|CAPTION= <scene name='initialview01'>2j5i</scene>, resolution 1.80&Aring;
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|SITE=
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|LIGAND=
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|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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2J5I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5I OCA].
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2J5I is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5I OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17139085 17139085]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17139085 17139085]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
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[[Category: vanillin]]
[[Category: vanillin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:59:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:37:29 2008''

Revision as of 15:37, 20 March 2008


PDB ID 2j5i

Drag the structure with the mouse to rotate
, resolution 1.80Å
Activity: Trans-feruloyl-CoA hydratase, with EC number 4.2.1.101
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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