Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli

Protein Science

Volumn 7, Issue 1, 1998, Pages 39-51

  Muchmore, Christine R A ^a,c   Krahn, Joseph M ^a   Kim, Jeong Hyun ^b,d   Zalkin, Howard ^b   Smith, Janet L ^a  

^a PURDUE UNIVERSITY   (United States)

^b PURDUE UNIVERSITY   (United States)

^c NORTHWESTERN UNIVERSITY   (United States)

^d Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

Allosteric enzyme; Complex enzyme; Fe S protein; Feedback inhibition; Glutamine amidotransferase; Phosphoribosyltransferase; Protein crystallography; Purine biosynthesis

Indexed keywords

AMIDOPHOSPHORIBOSYLTRANSFERASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ISOLATION; ENZYME STRUCTURE; ESCHERICHIA COLI; NEGATIVE FEEDBACK; NONHUMAN; PRIORITY JOURNAL; PURINE SYNTHESIS;

ESCHERICHIA COLI;

EID: 0031941411     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070104     Document Type: Article

References (46)

1. Allen FH, Kennard O. 1993. 3D search and research using the Cambridge Structural Database. Chemical Design Automation News 8:31-37.
2. Amann E, Ochs B, Abel KJ. 1988. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene 69:301-315.
3. Bolin JT, Smith JL, Muchmore SW. 1993. Considerations in phase refinement and extension: Experiments with a rapid and automatic procedure. Abstracts of the American Crystallographic Association 21:51.
4. Brannigan JA, Dodson G, Duggleby HJ, Moody PCE, Smith JL, Tomchick DR, Murzin AG. 1995. A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature 378:416-419.
5. Brünger AT. 1990. Extension of molecular replacement: A new search strategy based on Patterson correlation refinement. Acta Crystallogr A 46:46-57.
6. Brünger AT. 1991. Solution of a Fab (26-10)/digoxin complex by generalized molecular replacement. Acta Crystallogr A 47:195-204.
7. Brünger AT. 1992. X-PLOR, version 3.1. A system for X-ray crystallography and NMR. New Haven, Connecticut/London: Yale University Press.
8. Brünger AT, Krukowski A, Erickson JW. 1990. Slow-cooling protocols for crystallographic refinement by simulated annealing. Acta Crystallogr A 46:585-593.
9. CCP4. 1994. Collaborative Computational Project, Number 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50:760-763. [SERC Daresbury Laboratory, Bailey S, contact person.]
10. Chen S, Tomchick DR, Wolle D, Hu P, Smith JL, Switzer RL, Zalkin H. 1997. Mechanism of the synergistic endproduct regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphatc amidotransferase by nucleotides. Biochemistry 36:10718-10726.
11. Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC. 1994. The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell 78:325-334.
12. Hendrickson WA, Horton JR, Lemaster DM. 1990. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure. EMBO J 9:1665-1672.
13. Henriksen A, Aghajari N, Jensen KF, Gajhede M. 1996. A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase. Biochemistry 35:3803-3809.
14. Higashi T. 1989. The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography. J Appl Crystallogr 22:9-18.
15. Isupov MN, Obmolova G, Butterworth S, Badet-Denisot MA, Badet B, Polikarpov I, Littlechild JA, Teplyakov A. 1996. Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: Evidence from the 1.8 Å crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase. Structure 4:801-810.
16. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
17. Kabsch W. 1988. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J Appl Crystallogr 21:916-924.
18. Kim JH, Krahn JM, Tomchick DR, Smith JL, Zalkin H. 1996. Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J Biol Chem 271:15549-15557.
19. Kyte J. 1995. Structure in protein chemistry. New York/London: Garland Publishing, Inc. pp 64-69
20. McClard RW, Fischer AC, Mauldin SK, Jones ME. 1984. 5-Phosphorylribose 1-α-methylenebisphosphonate: Properties of a substrate analog of 5-phosphorylribose 1-α-diphosphate. Bioorganic Chem 12:339-348.
21. Messenger LJ, Zalkin H. 1979. Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli: Purification and properties. J Biol Chem 254:3382-3392.
22. Musick WDL. 1981. Structural features of the phosphoribosyltransferases and their relationship to the human deficiency disorders of purine and pyrimidine metabolism. CRC Crit Rev Biochem 11:1-34.
23. Otwinowski Z. 1991. Maximum likelihood refinement of heavy atom parameters. In: Wolf W, Evans PR, Leslie AGW, eds. Isomorphous replacement and anomalous scattering. Daresbury, England: Science & Engineering Research Council. pp 80-86.
24. Otwinowski Z. 1993. Oscillation data reduction program. In: Sawyer L, Isaacs N, Bailey S, eds. Data collection and processing. Daresbury, England: Science & Engineering Research Council. pp 56-62.
25. Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
26. Rossmann MG, Blow DM. 1962. The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallogr 15:24-31.
27. Rudolph J, Stubbe J. 1995. Investigation of the mechanism of phosphoribosylamine transfer from glutamine phosphoribosylpyrophosphate amidotransferase to glycinamide ribonucleotide synthetase. Biochemistry 34:2241-2250.
28. Sakabe N. 1991. X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl Inst Meth Phys Res A 303:448-463.
29. Scapin G, Grubmeyer C, Sacchettini JC. 1994. Crystal structure of orotate phosphoribosyltransferase. Biochemistry 33:1287-1294.
30. Scapin G, Ozturk DH, Grubmeyer C, Sacchettini JC. 1995. The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and α-D-5-phosphoribosyl-1-pyrophosphate. Biochemistry 34:10744-10754.
31. Schumacher MA, Carter D, Roos DS, Ullman B, Brennan RG. 1996. Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop. Nature Struct Biol 3:881-887.
32. Smith JL. 1995. Structures of glutamine amidotransferases from the purine biosynthetic pathway. Biochem Soc Trans 23:894-898.
33. Smith JL, Zaluzec EJ, Wery JP, Niu L, Switzer RL, Zalkin H, Satow Y. 1994. Structure of the allosteric regulatory enzyme of purine biosynthesis. Science 264:1427-1433.
34. Somoza JR, Chin MS, Focia PJ, Wang CC, Fletterick RJ. 1996. Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus. Biochemistry 35:7032-7040.
35. Stoker PW, O'Leary MH, Boehlein SK, Schuster SM, Richards NGJ. 1996. Probing the mechanism of nitrogen transfer in Escherichia coli asparagine synthetase by using heavy atom isotope effects. Biochemistry 35:3024-3030.
36. Switzer RL. 1989. Non-redox roles for iron-sulfur clusters in enzymes. BioFactors 2:77-86.
37. Tomchick DR, Smith JL, Wolle D, Zalkin H. 1994. Structure of B. subtilis glutamine PRPP amidotransferase at 2.3 Å and nucleotide binding studies. Abstracts of the ACA, Series 2, vol 22. p 49.
38. Tong L, Rossmann MG. 1990. The locked rotation function. Acta Crystallogr A 46:783-792.
39. Tronrud DE, Ten Eyck LF, Matthews BW. 1987. An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallogr A 43:489-501.
40. Vos S, de Jersey J, Martin JL. 1997. Crystal structure of Escherichia coli xanthine phosphoribosyltransferase. Biochemistry 36:4125-4134.
41. Wong JY, Bernlohr DA, Turnbough CL Jr, Switzer RL. 1981. Purification and properties of glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis. Biochemistry 20:5669-5674.
42. Wyngaarden JB. 1972. Glutamine phosphoribosylpyrophosphate amidotransferase. Curr Topics Cell Regulation 5:135-176.
43. Zalkin H. 1993. The amidotransferases. Adv Enzymol Relat Areas Mol Biol 66:203-309.
44. Zalkin H, Smith JL. 1998. Enzymes utilizing glutamine as an amide donor. Adv Enzymol Relat Areas Mol Biol 72. Forthcoming.
45. Zhou G, Charbonneau H, Colman RF, Zalkin H. 1993. Identification of sites for feedback regulation of glutamine 5-phosphoribosylpyrophosphate amidotransferase by nucleotides and relationship to residues important for catalysis. J Biol Chem 265:10471-10481.
46. Zhou G, Smith JL, Zalkin H. 1994. Binding of purine nucleotides to two regulatory sites results in synergistic feedback inhibition of glutamine 5-phosphoribosylpyrophosphate amidotransferase. J Biol Chem 269:6784-6789.