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2o7b

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[[Image:2o7b.jpg|left|200px]]
 
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{{Structure
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==Tyrosine ammonia-lyase from Rhodobacter sphaeroides, complexed with coumarate==
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|PDB= 2o7b |SIZE=350|CAPTION= <scene name='initialview01'>2o7b</scene>, resolution 1.60&Aring;
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<StructureSection load='2o7b' size='340' side='right'caption='[[2o7b]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=HC4:4'-HYDROXYCINNAMIC ACID'>HC4</scene>
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<table><tr><td colspan='2'>[[2o7b]] 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=2O7B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7B FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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|GENE= hutH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides])
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<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>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o7b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7b OCA], [https://pdbe.org/2o7b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7b RCSB], [https://www.ebi.ac.uk/pdbsum/2o7b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7b ProSAT]</span></td></tr>
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</table>
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'''Tyrosine ammonia-lyase from Rhodobacter sphaeroides, complexed with coumarate'''
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== Function ==
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[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>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o7b_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o7b ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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<ref>PMID:17185228</ref>
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2O7B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7B OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17185228 17185228]
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[[Category: Rhodobacter sphaeroides]]
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[[Category: Single protein]]
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[[Category: Baiga, T J.]]
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[[Category: Bowman, M E.]]
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[[Category: Louie, G V.]]
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[[Category: Moffitt, M C.]]
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[[Category: Moore, B S.]]
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[[Category: Noel, J P.]]
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[[Category: HC4]]
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[[Category: methylidene imidazolone prosthetic group]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:56:04 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2o7b" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Cereibacter sphaeroides]]
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[[Category: Large Structures]]
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[[Category: Baiga TJ]]
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[[Category: Bowman ME]]
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[[Category: Louie GV]]
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[[Category: Moffitt MC]]
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[[Category: Moore BS]]
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[[Category: Noel JP]]

Current revision

Tyrosine ammonia-lyase from Rhodobacter sphaeroides, complexed with coumarate

PDB ID 2o7b

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