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2o78

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Revision as of 07:04, 22 August 2018

Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant) complexed with cinnamic acid

Structural highlights

2o78 is a 8 chain structure with sequence from "rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	2o6y, 1gkm, 1w27, 1y2m, 1t6j, 2nyn
Gene:	hutH ("Rhodococcus capsulatus" Molisch 1907)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TALY_RHOS4] 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2o78"

@@ Line 1: / Line 1: @@
 ==Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant) complexed with cinnamic acid==
 <StructureSection load='2o78' size='340' side='right' caption='[[2o78]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <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='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>
-<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=2o78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o78 OCA], [http://pdbe.org/2o78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o78 RCSB], [http://www.ebi.ac.uk/pdbsum/2o78 PDBsum]</span></td></tr>
+<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=2o78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o78 OCA], [http://pdbe.org/2o78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o78 RCSB], [http://www.ebi.ac.uk/pdbsum/2o78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o78 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o78_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/2o78_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2o78

From Proteopedia

Revision as of 07:04, 22 August 2018

Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant) complexed with cinnamic acid

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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