2O7D

Tyrosine ammonia-lyase from Rhodobacter sphaeroides, complexed with caffeate

2O7D の概要

• エントリーDOI: 10.2210/pdb2o7d/pdb
• 関連するPDBエントリー: 1gkm 1t6j 1w27 1y2m 2nyn 2o6y
• 分子名称: Putative histidine ammonia-lyase, CAFFEIC ACID (3 entities in total)
• 機能のキーワード: methylidene imidazolone prosthetic group, lyase
• 由来する生物種: Rhodobacter sphaeroides
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 441006.76

構造登録者

Louie, G.V.,Bowman, M.E.,Moffitt, M.C.,Baiga, T.J.,Moore, B.S.,Noel, J.P. (登録日: 2006-12-10, 公開日: 2007-01-16, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)