2o7f: Difference between revisions

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-{{Seed}}
-[[Image:2o7f.png|left|200px]]
-<!--
+==Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), complexed with coumaric acid==
-The line below this paragraph, containing "STRUCTURE_2o7f", creates the "Structure Box" on the page.
+<StructureSection load='2o7f' size='340' side='right'caption='[[2o7f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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>
-{{STRUCTURE_2o7f|  PDB=2o7f  |  SCENE=  }}
+<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>
+</table>
+== 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o7f_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=2o7f ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), complexed with coumaric acid===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_17185228}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2o7f" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 17185228 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17185228}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Cereibacter sphaeroides]]
-O7F is a 8 chains structure of sequences 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=2O7F OCA].
+[[Category: Large Structures]]
+[[Category: Baiga TJ]]
-==Reference==
+[[Category: Bowman ME]]
-<ref group="xtra">PMID:17185228</ref><references group="xtra"/>
+[[Category: Louie GV]]
-[[Category: Rhodobacter sphaeroides]]
+[[Category: Moffitt MC]]
-[[Category: Baiga, T J.]]
+[[Category: Moore BS]]
-[[Category: Bowman, M E.]]
+[[Category: Noel JP]]
-[[Category: Louie, G V.]]
-[[Category: Moffitt, M C.]]
-[[Category: Moore, B S.]]
-[[Category: Noel, J P.]]
-[[Category: Methylidene imidazolone prosthetic group]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 06:50:59 2009''