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2o7b
From Proteopedia
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|PDB= 2o7b |SIZE=350|CAPTION= <scene name='initialview01'>2o7b</scene>, resolution 1.60Å | |PDB= 2o7b |SIZE=350|CAPTION= <scene name='initialview01'>2o7b</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HC4:4 | + | |LIGAND= <scene name='pdbligand=HC4:4'-HYDROXYCINNAMIC ACID'>HC4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= hutH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | |GENE= hutH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 Rhodobacter sphaeroides]) | ||
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[[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 Sun Mar 23 15:31:15 2008'' |
Revision as of 13:31, 23 March 2008
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| , resolution 1.60Å | |||||||
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| Ligands: | |||||||
| Gene: | hutH (Rhodobacter sphaeroides) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Tyrosine ammonia-lyase from Rhodobacter sphaeroides, complexed with coumarate
Overview
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
2O7B is a Single protein structure of sequence from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 23 15:31:15 2008
