2j5i: Difference between revisions
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==Crystal Structure of Hydroxycinnamoyl-CoA Hydratase-Lyase== | ==Crystal Structure of Hydroxycinnamoyl-CoA Hydratase-Lyase== | ||
<StructureSection load='2j5i' size='340' side='right' caption='[[2j5i]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2j5i' size='340' side='right'caption='[[2j5i]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2j5i]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. 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:// | <table><tr><td colspan='2'>[[2j5i]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_liquefaciens"_flugge_1886 "bacillus fluorescens liquefaciens" flugge 1886]. 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://proteopedia.org/fgij/fg.htm?mol=2J5I FirstGlance]. <br> | ||
</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> | </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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2j5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j5i OCA], [http://pdbe.org/2j5i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j5i RCSB], [http://www.ebi.ac.uk/pdbsum/2j5i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j5i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus fluorescens liquefaciens flugge 1886]] | [[Category: Bacillus fluorescens liquefaciens flugge 1886]] | ||
[[Category: Large Structures]] | |||
[[Category: Trans-feruloyl-CoA hydratase]] | [[Category: Trans-feruloyl-CoA hydratase]] | ||
[[Category: Brzozowski, A M]] | [[Category: Brzozowski, A M]] | ||
Revision as of 10:41, 15 April 2020
Crystal Structure of Hydroxycinnamoyl-CoA Hydratase-LyaseCrystal Structure of Hydroxycinnamoyl-CoA Hydratase-Lyase
Structural highlights
Function[HCHL_PSEFL] Catalyzes the hydration of the acyl-CoA thioester of ferulic acid and the subsequent retro-aldol cleavage of the hydrated intermediate to yield vanillin (4-hydroxy-3-methoxy-benzaldehyde).[1] 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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