2fs2

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spinqualitylabelsall models 2fs2, resolution 2.000Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

2FS2 is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. Full crystallographic information is available from OCA.

Reference

Structure, function, and mechanism of the phenylacetate pathway hot dog-fold thioesterase PaaI., Song F, Zhuang Z, Finci L, Dunaway-Mariano D, Kniewel R, Buglino JA, Solorzano V, Wu J, Lima CD, J Biol Chem. 2006 Apr 21;281(16):11028-38. Epub 2006 Feb 7. PMID:16464851

Page seeded by OCA on Wed Nov 21 10:43:55 2007