2O7F

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

Summary for 2O7F

• Entry DOI: 10.2210/pdb2o7f/pdb
• Related: 1gkm 1t6j 1w27 1y2m 2nyn 2o6y
• Descriptor: Putative histidine ammonia-lyase, 4'-HYDROXYCINNAMIC ACID (3 entities in total)
• Functional Keywords: methylidene imidazolone prosthetic group, lyase
• Biological source: Rhodobacter sphaeroides
• Total number of polymer chains: 8
• Total formula weight: 440950.98

Authors

Louie, G.V.,Bowman, M.E.,Moffitt, M.C.,Baiga, T.J.,Moore, B.S.,Noel, J.P. (deposition date: 2006-12-11, release date: 2007-01-16, Last modification date: 2023-11-15)

Primary citation

Louie, G.V.,Bowman, M.E.,Moffitt, M.C.,Baiga, T.J.,Moore, B.S.,Noel, J.P.
Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.
Chem.Biol., 13:1327-1338, 2006

PubMed Abstract: 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.

PubMed: 17185228
DOI: 10.1016/j.chembiol.2006.11.011

Experimental method

X-RAY DIFFRACTION (2 Å)