1PSU

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

Summary for 1PSU

• Entry DOI: 10.2210/pdb1psu/pdb
• Descriptor: Phenylacetic acid degradation protein PaaI (2 entities in total)
• Functional Keywords: structural genomics, nysgxrc, t820, phenylacetic acid, degradation, operon, psi, protein structure initiative, new york sgx research center for structural genomics, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 30200.41

Authors

Kniewel, R.,Buglino, J.,Solorzano, V.,Wu, J.,Lima, C.D.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2003-06-21, release date: 2003-07-08, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)