2o7e: Difference between revisions
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<StructureSection load='2o7e' size='340' side='right'caption='[[2o7e]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='2o7e' size='340' side='right'caption='[[2o7e]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2o7e]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2o7e]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7E FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene>, <scene name='pdbligand=PMI:(2-AMINO-2,3-DIHYDRO-1H-INDEN-2-YL)PHOSPHONIC+ACID'>PMI</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7e OCA], [https://pdbe.org/2o7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7e RCSB], [https://www.ebi.ac.uk/pdbsum/2o7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7e ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7e OCA], [https://pdbe.org/2o7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7e RCSB], [https://www.ebi.ac.uk/pdbsum/2o7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TALY_CERS4 TALY_CERS4] Catalyzes the non-oxidative deamination of L-tyrosine. Has very low phenylalanine ammonia-lyase activity (in vitro).<ref>PMID:17185228</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cereibacter sphaeroides]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Baiga | [[Category: Baiga TJ]] | ||
[[Category: Bowman | [[Category: Bowman ME]] | ||
[[Category: Louie | [[Category: Louie GV]] | ||
[[Category: Moffitt | [[Category: Moffitt MC]] | ||
[[Category: Moore | [[Category: Moore BS]] | ||
[[Category: Noel | [[Category: Noel JP]] | ||
Revision as of 13:32, 30 August 2023
Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), bound to 2-aminoindan-2-phosphonic acidTyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), bound to 2-aminoindan-2-phosphonic acid
Structural highlights
FunctionTALY_CERS4 Catalyzes the non-oxidative deamination of L-tyrosine. Has very low phenylalanine ammonia-lyase activity (in vitro).[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 PubMedAromatic amino acid ammonia-lyases catalyze the deamination of L-His, L-Phe, and L-Tyr, yielding ammonia plus aryl acids bearing an alpha,beta-unsaturated propenoic acid. We report crystallographic analyses of unliganded Rhodobacter sphaeroides tyrosine ammonia-lyase (RsTAL) and RsTAL bound to p-coumarate and caffeate. His 89 of RsTAL forms a hydrogen bond with the p-hydroxyl moieties of coumarate and caffeate. His 89 is conserved in TALs but replaced in phenylalanine ammonia-lyases (PALs) and histidine ammonia-lyases (HALs). Substitution of His 89 by Phe, a characteristic residue of PALs, yields a mutant with a switch in kinetic preference from L-Tyr to L-Phe. Structures of the H89F mutant in complex with the PAL product, cinnamate, or the PAL-specific inhibitor, 2-aminoindan-2-phosphonate (AIP), support the role of position 89 as a specificity determinant in the family of aromatic amino acid ammonia-lyases and aminomutases responsible for beta-amino acid biosynthesis. Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.,Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP Chem Biol. 2006 Dec;13(12):1327-38. PMID:17185228[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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