2o7e: Difference between revisions
New page: left|200px<br /><applet load="2o7e" size="350" color="white" frame="true" align="right" spinBox="true" caption="2o7e, resolution 1.75Å" /> '''Tyrosine ammonia-lya... |
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==Overview== | ==Overview== | ||
Aromatic amino acid ammonia-lyases catalyze the deamination of L-His, L-Phe, and L-Tyr, yielding ammonia plus aryl acids bearing an | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baiga, T | [[Category: Baiga, T J.]] | ||
[[Category: Bowman, M | [[Category: Bowman, M E.]] | ||
[[Category: Louie, G | [[Category: Louie, G V.]] | ||
[[Category: Moffitt, M | [[Category: Moffitt, M C.]] | ||
[[Category: Moore, B | [[Category: Moore, B S.]] | ||
[[Category: Noel, J | [[Category: Noel, J P.]] | ||
[[Category: PMI]] | [[Category: PMI]] | ||
[[Category: methylidene imidazolone prosthetic group]] | [[Category: methylidene imidazolone prosthetic group]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:15:20 2008'' | ||
Revision as of 19:15, 21 February 2008
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Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant), bound to 2-aminoindan-2-phosphonic acid
OverviewOverview
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.
About this StructureAbout this Structure
2O7E is a Single protein structure of sequence from Rhodobacter sphaeroides with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
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