This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2o6y

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:37, 28 July 2021

Tyrosine ammonia-lyase from Rhodobacter sphaeroides

Structural highlights

2o6y is a 8 chain structure with sequence from "luteovulum_sphaeroides"_(van_niel_1944)_suresh_et_al._2019 "luteovulum sphaeroides" (van niel 1944) suresh et al. 2019. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1gkm, 1w27, 1y2m, 1t6j, 2nyn
Gene:	hutH ("Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019)
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/2o6y"

@@ Line 3: / Line 3: @@
 <StructureSection load='2o6y' size='340' side='right'caption='[[2o6y]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2o6y]] is a 8 chain structure with sequence from [https://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=2O6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O6Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2o6y]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/"luteovulum_sphaeroides"_(van_niel_1944)_suresh_et_al._2019 "luteovulum sphaeroides" (van niel 1944) suresh et al. 2019]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O6Y FirstGlance]. <br>
 </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gkm|1gkm]], [[1w27|1w27]], [[1y2m|1y2m]], [[1t6j|1t6j]], [[2nyn|2nyn]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hutH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hutH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019])</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=2o6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o6y OCA], [https://pdbe.org/2o6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o6y RCSB], [https://www.ebi.ac.uk/pdbsum/2o6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o6y ProSAT]</span></td></tr>
 </table>
@@ Line 34: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Rhodococcus capsulatus molisch 1907]]
 [[Category: Large Structures]]
 [[Category: Baiga, T J]]

2o6y

From Proteopedia

Revision as of 10:37, 28 July 2021

Tyrosine ammonia-lyase from Rhodobacter sphaeroides

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox