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| | ==Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), complexed with coumaric acid== | | ==Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), complexed with coumaric acid== |
| - | <StructureSection load='2o7f' size='340' side='right' caption='[[2o7f]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2o7f' size='340' side='right'caption='[[2o7f]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2o7f]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2O7F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2o7f]] 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=2O7F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7F FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HC4:4-HYDROXYCINNAMIC+ACID'>HC4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HC4:4-HYDROXYCINNAMIC+ACID'>HC4</scene>, <scene name='pdbligand=MDO:{2-[(1S)-1-AMINOETHYL]-4-METHYLIDENE-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>MDO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o6y|2o6y]], [[1gkm|1gkm]], [[1w27|1w27]], [[1y2m|1y2m]], [[1t6j|1t6j]], [[2nyn|2nyn]]</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=2o7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7f OCA], [https://pdbe.org/2o7f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7f RCSB], [https://www.ebi.ac.uk/pdbsum/2o7f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7f ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hutH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907])</td></tr>
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| - | <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=2o7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7f OCA], [http://pdbe.org/2o7f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o7f RCSB], [http://www.ebi.ac.uk/pdbsum/2o7f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7f ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TALY_RHOS4 TALY_RHOS4]] Catalyzes the non-oxidative deamination of L-tyrosine. Has very low phenylalanine ammonia-lyase activity (in vitro).<ref>PMID:17185228</ref> | + | [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: Rhodococcus capsulatus molisch 1907]] | + | [[Category: Cereibacter sphaeroides]] |
| - | [[Category: Baiga, T J]] | + | [[Category: Large Structures]] |
| - | [[Category: Bowman, M E]] | + | [[Category: Baiga TJ]] |
| - | [[Category: Louie, G V]] | + | [[Category: Bowman ME]] |
| - | [[Category: Moffitt, M C]] | + | [[Category: Louie GV]] |
| - | [[Category: Moore, B S]] | + | [[Category: Moffitt MC]] |
| - | [[Category: Noel, J P]] | + | [[Category: Moore BS]] |
| - | [[Category: Lyase]] | + | [[Category: Noel JP]] |
| - | [[Category: Methylidene imidazolone prosthetic group]]
| + | |
| Structural highlights
Function
TALY_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 PubMed
Aromatic 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
- ↑ Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP. Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases. Chem Biol. 2006 Dec;13(12):1327-38. PMID:17185228 doi:10.1016/j.chembiol.2006.11.011
- ↑ Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP. Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases. Chem Biol. 2006 Dec;13(12):1327-38. PMID:17185228 doi:10.1016/j.chembiol.2006.11.011
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