2FS2

Structure of the E. coli PaaI protein from the phyenylacetic acid degradation operon

2FS2 の概要

• エントリーDOI: 10.2210/pdb2fs2/pdb
• 関連するPDBエントリー: 1PSU
• 分子名称: Phenylacetic acid degradation protein paaI, SULFATE ION (3 entities in total)
• 機能のキーワード: t820, phenylacetic acid, degradation, operon, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32851.24

構造登録者

Kniewel, R.,Buglino, J.A.,Solorzano, V.,Wu, J.,Lima, C.D.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2006-01-20, 公開日: 2006-02-07, 最終更新日: 2024-10-16)

主引用文献

Song, F.,Zhuang, Z.,Finci, L.,Dunaway-Mariano, D.,Kniewel, R.,Buglino, J.A.,Solorzano, V.,Wu, J.,Lima, C.D.
Structure, Function, and Mechanism of the Phenylacetate Pathway Hot Dog-fold Thioesterase PaaI
J.Biol.Chem., 281:11028-11038, 2006

PubMed Abstract: The structure and biochemical function of the hot dog-fold thioesterase PaaI operative in the aerobic phenylacetate degradation pathway are examined. PaaI showed modest activity with phenylacetyl-coenzyme A, suggestive of a role in coenzyme A release from this pathway intermediate in the event of limiting downstream pathway enzymes. Minimal activity was observed with aliphatic acyl-coenzyme A thioesters, which ruled out PaaI function in the lower phenylacetate pathway. PaaI was most active with ring-hydroxylated phenylacetyl-coenzyme A thioesters. The x-ray crystal structure of the Escherichia coli thioesterase is reported and analyzed to define the structural basis of substrate recognition and catalysis. The contributions of catalytic and substrate binding residues, thus, identified were examined through steady-state kinetic analysis of site-directed mutant proteins.

PubMed: 16464851
DOI: 10.1074/jbc.M513896200

実験手法

X-RAY DIFFRACTION (2 Å)