The Pathway of Product Release from the R State of Aspartate Transcarbamoylase

Journal of Molecular Biology

Volumn 401, Issue 5, 2010, Pages 940-948

  Mendes, Kimberly R ^a   Kantrowitz, Evan R ^a  

^a BOSTON COLLEGE   (United States)

Author keywords

Allosteric transition; Cooperativity; Enzyme mechanism; Protein structure function; X ray crystallography

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; CARBAMOYL PHOSPHATE; PHOSPHATE; SPARFOSIC ACID;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; DISULFIDE BOND; ENZYME ANALYSIS; ENZYME BINDING; ENZYME RELEASE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; MOLECULE; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS; WILD TYPE;

ESCHERICHIA COLI;

EID: 77955550578     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.07.003     Document Type: Article

References (39)

1. Gerhart J.C., Pardee A.B. Enzymology of control by feedback inhibition. J. Biol. Chem. 1962, 237:891-896.
2. Wild J.R., Loughrey-Chen S.J., Corder T.S. In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamylase. Proc. Natl Acad. Sci. USA 1989, 86:46-50.
3. Weber K.K. New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain. Nature 1968, 218:1116-1119.
4. Wiley D.C., Lipscomb W.N. Crystallographic determination of symmetry of aspartate transcarbamylase. Nature 1968, 218:1119-1121.
5. Gerhart J.C., Schachman H.K. Allosteric interactions in aspartate transcarbamylase: II. Evidence for different conformational states of the protein in the presence and absence of specific ligands. Biochemistry 1968, 7:538-552.
6. Howlett G.J., Blackburn M.N., Compton J.G., Schachman H.K. Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model. Biochemistry 1977, 16:5091-5099.
7. Kantrowitz E.R., Lipscomb W.N. Escherichia coli aspartate transcarbamylase: the relations between structure and function. Science 1988, 241:669-674.
8. Ke H.M., Lipscomb W.N., Cho Y., Honzatko R.B. Complex of N-phosphonacetyl-l-aspartate with aspartate carbamoyltransferase: X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms. J. Mol. Biol. 1988, 204:725-747.
9. Ladjimi M.M., Kantrowitz E.R. A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies. Biochemistry 1988, 27:276-283.
10. Tsuruta H., Sano T., Vachette P., Tauc P., Moody M.F., Wakabayashi K., et al. Structural kinetics of the allosteric transition of aspartate transcarbamoylase produced by physiological substrates. FEBS Lett. 1990, 263:66-68.
11. Tsuruta H., Vachette P., Sano T., Moody M.F., Tauc P., Amemiya Y., et al. Kinetics of the quaternary structure change of aspartate transcarbamoylase triggered by succinate, a competitive inhibitor. Biochemistry 1994, 33:10007-10012.
12. Huang J., Lipscomb W.N. Products in the T-state of aspartate transcarbamylase: crystal structure of the phosphate and N-carbamyl-l-aspartate ligated enzyme. Biochemistry 2004, 43:6422-6426.
13. West J.M., Tsuruta H., Kantrowitz E.R. Stabilization of the R allosteric structure of E. coli aspartate transcarbamoylase by disulfide bond formation. J. Biol. Chem. 2002, 277:47300-47304.
14. Wang J., Stieglitz K.A., Cardia J.P., Kantrowitz E.R. Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase. Proc. Natl Acad. Sci. USA 2005, 102:8881-8886.
15. Stieglitz K.A., Dusinberre K.J., Cardia J.P., Tsuruta H., Kantrowitz E.R. Structure of the E. coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle. J. Mol. Biol. 2005, 352:478-486.
16. Wang J., Eldo J., Kantrowitz E.R. Structural model of the R state of Escherichia coli aspartate transcarbamoylase with substrates bound. J. Mol. Biol. 2007, 371:1261-1273.
17. Jin L., Stec B., Lipscomb W.N., Kantrowitz E.R. Insights into the mechanism of catalysis and heterotropic regulation of E. coli aspartate transcarbamoylase based upon a structure of enzyme complexed with the bisubstrate analog N-phosphonacetyl-l-aspartate at 2.1 Å. Proteins Struct. Funct. Genet. 1999, 37:729-742.
18. Huang J., Lipscomb W.N. Aspartate transcarbamylase (ATCase) of Escherichia coli: a new crystalline R-state bound to PALA, or to product analogues citrate and phosphate. Biochemistry 2004, 43:6415-6421.
19. Chan R.S., Sakash J.B., Macol C.P., West J.M., Tsuruta H., Kantrowitz E.R. The role of intersubunit interactions for the stabilization of the T state of Escherichia coli aspartate transcarbamoylase. J. Biol. Chem. 2002, 277:49755-49760.
20. Tauc P., Vachette P., Middleton S.A., Kantrowitz E.R. The structural consequences of a single amino acid mutation on aspartate transcarbamylase from Escherichia coli. J. Mol. Biol. 1990, 214:327-335.
21. Fetler L., Vachette P., Hervé G., Ladjimi M.M. Unlike the quaternary structure transition, the tertiary structure change of the 240's loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion. Biochemistry 1995, 34:15654-15660.
22. Hsuanyu Y., Wedler F.C. Kinetic mechanism of native Escherichia coli aspartate transcarbamylase. Arch. Biochem. Biophys. 1987, 259:316-330.
23. Wedler F.C., Gasser F.J. Ordered substrate binding and evidence for a thermally induced change in mechanism for E. coli aspartate transcarbamylase. Arch. Biochem. Biophys. 1974, 163:57-68.
24. Adams P.D., Grosse-Kunstleve R.W., Hung L.W., Ioerger T.R., McCoy A.J., Moriarty N.W., et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. Sect. D 2002, 58:1948-1954.
25. Kosman R.P., Gouaux J.E., Lipscomb W.N. Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 Å resolution: implications for aspartate transcarbamoylase mutants and the mechanism of negative cooperativity. Proteins Struct. Funct. Genet. 1993, 15:147-176.
26. Stieglitz K., Stec B., Baker D.P., Kantrowitz E.R. Monitoring the transition from the T to the R state in E. coli aspartate transcarbamoylase by X-ray crystallography: crystal structures of the E50A mutant in four distinct allosteric states. J. Mol. Biol. 2004, 341:853-868.
27. DeLano W.L. The PyMOL Molecular Graphics System 2002, DeLano Scientific LLC, San Carlos, CA. http://www.pymol.org.
28. Gouaux J.E., Stevens R.C., Lipscomb W.N. Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate and CTP or ATP at 2.8 Å resolution and neutral pH. Biochemistry 1990, 29:7702-7715.
29. Nowlan S.F., Kantrowitz E.R. Superproduction and rapid purification of E. coli aspartate transcarbamoylase and its catalytic subunit under extreme derepression of the pyrimidine pathway. J. Biol. Chem. 1985, 260:14712-14716.
30. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
31. Davis B.J. Disc electrophoresis: II. Method and application to human serum proteins. Ann. NY Acad. Sci. 1964, 121:404-427.
32. Ornstein L. Disc electrophoresis: I. Background and theory. Ann. NY Acad. Sci. 1964, 121:321-349.
33. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
34. Pastra-Landis S.C., Foote J., Kantrowitz E.R. An improved colorimetric assay for aspartate and ornithine transcarbamylases. Anal. Biochem. 1981, 118:358-363.
35. Silver R.S., Daigneault J.P., Teague P.D., Kantrowitz E.R. Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions. J. Mol. Biol. 1983, 168:729-745.
36. Pastra-Landis S.C., Evans D.R., Lipscomb W.N. The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli. J. Biol. Chem. 1978, 253:4624-4630.
37. McCoy A.J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. Sect. D 2007, 63:32-41.
38. Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 2004, 60:2126-2132.
39. Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 1993, 26:283-291.