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The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate.
Biochemistry. 1995 Aug 29; 34(34):10744-54.B

Abstract

The three-dimensional structure of Salmonella typhimurium orotate phosphoribosyltransferase (OPRTase) in complex with the ribose 5-phosphate donor alpha-D-5--phosphoribosyl-1-pyrophosphate (PRPP) and the nitrogenous base orotic acid has been solved and refined with X-ray diffraction data extending to 2.3 A resolution to a crystallographic R-factor of 18.7%. The complex was generated by carrying out catalysis in the crystal. Comparison of this structure with the previously reported structure of the orotidine 5'-monophosphate (OMP) complex [Scapin, G., Grubmeyer, C., and Sacchettini, J. C. (1994) Biochemistry 33, 1287-1294] revealed that the enzyme backbone undergoes only small movements. The most significant differences occur near the active site, at Ala71-Gly74, with the largest difference involving the side chains of Lys73, Val127-Ala133, the 5'-phosphate binding loop, and a long, solvent-exposed loop at the dimer interface. The position of the ribose moiety is, on the other hand, very different in the OMP and PRPP.orotate complexes, with its anomeric carbon moving approximately 7 A across the binding cavity. In the PRPP.orotate complex the highly conserved acidic side chain of Asp124 interacts with the ribose of PRPP, whereas there are no interactions of this aspartate with the substrate in the OMP complex.

Authors+Show Affiliations

Scapin G
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Ozturk DH
No affiliation info available
Grubmeyer C
No affiliation info available
Sacchettini JC
No affiliation info available

MeSH

Binding SitesComputer GraphicsCrystallizationCrystallography, X-RayModels, MolecularMolecular StructureOrotate PhosphoribosyltransferaseOrotic AcidPhosphoribosyl PyrophosphateProtein ConformationProtein Structure, TertiarySalmonella typhimuriumUridine Monophosphate

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7545004

Citation

Scapin, G, et al. "The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed With Orotate and Alpha-D-5-phosphoribosyl-1-pyrophosphate." Biochemistry, vol. 34, no. 34, 1995, pp. 10744-54.
Scapin G, Ozturk DH, Grubmeyer C, et al. The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate. Biochemistry. 1995;34(34):10744-54.
Scapin, G., Ozturk, D. H., Grubmeyer, C., & Sacchettini, J. C. (1995). The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate. Biochemistry, 34(34), 10744-54.
Scapin G, et al. The Crystal Structure of the Orotate Phosphoribosyltransferase Complexed With Orotate and Alpha-D-5-phosphoribosyl-1-pyrophosphate. Biochemistry. 1995 Aug 29;34(34):10744-54. PubMed PMID: 7545004.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate. AU - Scapin,G, AU - Ozturk,D H, AU - Grubmeyer,C, AU - Sacchettini,J C, PY - 1995/8/29/pubmed PY - 1995/8/29/medline PY - 1995/8/29/entrez SP - 10744 EP - 54 JF - Biochemistry JO - Biochemistry VL - 34 IS - 34 N2 - The three-dimensional structure of Salmonella typhimurium orotate phosphoribosyltransferase (OPRTase) in complex with the ribose 5-phosphate donor alpha-D-5--phosphoribosyl-1-pyrophosphate (PRPP) and the nitrogenous base orotic acid has been solved and refined with X-ray diffraction data extending to 2.3 A resolution to a crystallographic R-factor of 18.7%. The complex was generated by carrying out catalysis in the crystal. Comparison of this structure with the previously reported structure of the orotidine 5'-monophosphate (OMP) complex [Scapin, G., Grubmeyer, C., and Sacchettini, J. C. (1994) Biochemistry 33, 1287-1294] revealed that the enzyme backbone undergoes only small movements. The most significant differences occur near the active site, at Ala71-Gly74, with the largest difference involving the side chains of Lys73, Val127-Ala133, the 5'-phosphate binding loop, and a long, solvent-exposed loop at the dimer interface. The position of the ribose moiety is, on the other hand, very different in the OMP and PRPP.orotate complexes, with its anomeric carbon moving approximately 7 A across the binding cavity. In the PRPP.orotate complex the highly conserved acidic side chain of Asp124 interacts with the ribose of PRPP, whereas there are no interactions of this aspartate with the substrate in the OMP complex. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/7545004/The_crystal_structure_of_the_orotate_phosphoribosyltransferase_complexed_with_orotate_and_alpha_D_5_phosphoribosyl_1_pyrophosphate_ L2 - https://www.yeastgenome.org/reference/7545004 DB - PRIME DP - Unbound Medicine ER -