2j5i: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2j5i]] is a 12 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J5I FirstGlance]. <br> | <table><tr><td colspan='2'>[[2j5i]] is a 12 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J5I FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2j5i RCSB], [http://www.ebi.ac.uk/pdbsum/2j5i PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=2j5i RCSB], [http://www.ebi.ac.uk/pdbsum/2j5i PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Pseudomonas fluorescens]] | [[Category: Pseudomonas fluorescens]] | ||
[[Category: Trans-feruloyl-CoA hydratase]] | [[Category: Trans-feruloyl-CoA hydratase]] | ||
[[Category: Brzozowski, A M | [[Category: Brzozowski, A M]] | ||
[[Category: Grogan, G | [[Category: Grogan, G]] | ||
[[Category: Lebedev, A | [[Category: Lebedev, A]] | ||
[[Category: Leonard, P M | [[Category: Leonard, P M]] | ||
[[Category: Marshall, C M | [[Category: Marshall, C M]] | ||
[[Category: Smith, D J | [[Category: Smith, D J]] | ||
[[Category: Verma, C S | [[Category: Verma, C S]] | ||
[[Category: Walton, N J | [[Category: Walton, N J]] | ||
[[Category: Aldolase]] | [[Category: Aldolase]] | ||
[[Category: Coenzyme-a]] | [[Category: Coenzyme-a]] | ||
Revision as of 20:20, 19 January 2015
CRYSTAL STRUCTURE OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASECRYSTAL STRUCTURE OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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