PMID: 6406227Jun 1, 1983Paper

p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. 2. Fitting of the amino-acid sequence to the tertiary structure

European Journal of Biochemistry
W J WeijerJ Drenth

Abstract

The complete primary and tertiary structure of p-hydroxybenzoate hydroxylase is now known. The amino acid sequences of the two largest CNBr peptides have been fitted to the electron-density map at 0.25-nm resolution. The parts of the polypeptide chain contributing the residues to the FAD-binding site and the residues of the substrate-binding site have been identified. The active site is located in a large hydrophobic area enclosed by all domains of the enzyme structure. Here the substrate, p-hydroxybenzoate, is bound near, but not in direct contact with, the isoalloxazine ring system of FAD. Many side chains from the C-terminal part of the polypeptide chain are involved in subunit-subunit interactions. In the center of one of the largely hydrophobic contact areas between the subunits, a cluster of six aromatic amino acids was found.

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Citations

Jan 1, 1985·Progress in Biophysics and Molecular Biology·W G Hol
Jan 1, 1987·Free Radical Biology & Medicine·F Müller
Jul 8, 1997·Proceedings of the National Academy of Sciences of the United States of America·P ChaiyenV Massey
Apr 15, 1989·European Journal of Biochemistry·S Ghisla, V Massey
Jan 12, 1990·European Journal of Biochemistry·T SejlitzH Y Neujahr
Feb 1, 1991·Journal of Protein Chemistry·T Sejlitz, H Y Neujahr
Dec 25, 2010·Physical Chemistry Chemical Physics : PCCP·Yan-Wen Tan, Haw Yang
Feb 16, 2021·Biotechnology Advances·Caroline E PaulWillem J H van Berkel
Aug 1, 1986·Biophysical Chemistry·A P Korn
Sep 27, 1990·Biochimica Et Biophysica Acta·K Suzuki, K Ohnishi
Dec 8, 2004·Archives of Biochemistry and Biophysics·Barrie EntschDavid P Ballou
Feb 28, 1985·Biochemical and Biophysical Research Communications·M HaniuJ E Shively
Sep 5, 2009·Archives of Biochemistry and Biophysics·Pimchai Chaiyen

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