Structure and function of Salmonella typhimurium orotate phosphoribosyltransferase: protein complementation reveals shared active sites

Biochemistry
D OzturkC Grubmeyer

Abstract

A solvent-exposed loop, comprising residues 98-119 of S. typhimurium orotate phosphoribosyltransferase (OPRTase), is at the subunit interface of the dimeric enzyme, and its amino acid side chains potentially contact active sites on either subunit. A portion of the loop (103-107) appears to be mobile on the basis of the X-ray structures of enzyme.OMP [Scapin, G., Grubmeyer, C., & Sacchettini, J. C. (1994) Biochemistry 33, 1287-1294] and enzyme.PRPP.orotate complexes [Scapin, G., Ozturk, D. H., Grubmeyer, C., & Sacchettini, J. C. (1995) Biochemistry 34, 10744-10754]. Lys-103, which is essential for activity [Ozturk, D. H., Dorfman, R. H. Scapin, G., Sacchettini, J. C., & Grubmeyer, C. (1995) Biochemistry 34, 10755-10763], may thus be functional in the active site formed by the adjacent subunit. Asp-125 is an essential residue that is in the middle of the active site. Equimolar mixtures of the nearly inactive K103A and D125N mutant ORPTase subunits produced approximately 21-23% of the enzymatic activity of the wild-type OPRTase. Heterodimer formation in the complemented mixtures was evidenced by various physical methods. Thus, the active site of OPRTase requires Asp-125 from one subunit and Lys-103 from the adjacent subunit. As pr...Continue Reading

Citations

Dec 26, 2001·Current Opinion in Structural Biology·S C Sinha, J L Smith
Apr 26, 2012·Biochemistry·Gary P WangCharles Grubmeyer
Apr 26, 2012·Biochemistry·Charles GrubmeyerSteven C Almo
Nov 23, 2013·Archives of Biochemistry and Biophysics·Michael Riis HansenJakob R Winther
Jan 5, 2002·Proceedings of the National Academy of Sciences of the United States of America·Maria A SchumacherRichard G Brennan
Feb 3, 2007·Journal of Theoretical Biology·Marcio S de Queiroz, Grover L Waldrop
Dec 20, 2016·Scientific Reports·Tomohiro SuzukiHirokazu Kawagishi
Sep 1, 2008·EcoSal Plus·Kaj Frank JensenMartin WillemoËs

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