Large differences are observed between the crystal and solution quaternary structures of allosteric aspartate transcarbamylase in the R state

Proteins: Structure, Function and Genetics

Volumn 27, Issue 1, 1997, Pages 110-117

  Svergun, Dmitri I ^a,b   Barberato, Claudio ^a,d   Koch, Michel H J ^a   Fetler, Luc ^c   Vachette, Patrice ^c  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b SHUBNIKOV INSTITUTE OF CRYSTALLOGRAPHY   (Russian Federation)

^c UNIVERSITÉ PARIS SACLAY   (France)

^d LABORATÓRIO NACIONAL DE LUZ SÍNCROTRON   (Brazil)

Author keywords

allosteric enzymes; crystal structure; rigid body modeling; small angle scattering; x rays

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE;

ALLOSTERISM; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME ISOLATION; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE;

ALLOSTERIC SITE; ASPARTATE CARBAMOYLTRANSFERASE; ESCHERICHIA COLI; PROTEIN CONFORMATION; SCATTERING, RADIATION; X-RAYS;

ESCHERICHIA COLI; TRIXIS;

EID: 0031027047     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199701)27:1<110::AID-PROT11>3.0.CO;2-Q     Document Type: Article

References (29)

1. Stryer, L. "Biochemistry." New York: W.H. Freeman, 1995.
2. Reichard, P., Hanshoff, G. Aspartate carbamyl transferase from Escherichia coli. Acta Chim. Scand. 10:548-566, 1956.
3. Yates, R.A., Pardee, A.B. Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism. J. Biol. Chem. 221:757-770, 1956.
4. Kantrowitz, E.R., Lipscomb, W.N. Escherichia coli aspartate transcarbamylase: The relation between structure and function. Science 241:669-674, 1988.
5. Stevens, R.C., Gouaux, J.E., Lipscomb, W.N. Structural consequences of effector binding to the T state of aspartate carbamoytransferase: Crystal structures of the unligated and ATP and CTP-complexed enzymes at 2.6 A resolution. Biochemistry 29:7691-7701, 1990.
6. Lipscomb, W.N. Aspartate transcarbamoylase from Escherichia coli: activity and regulation. Adv. Enzymol. 68: 67-151, 1994.
7. Monod, J., Wyman, J., Changeux, J.P. On the nature of allosteric transitions. A plausible model. J. Mol. Biol. 12: 88-118, 1965.
8. 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 7:538-552, 1968.
9. Howlett, G.J., Schachmann, H.K. Allosteric regulation of aspartate transcarbamoylase: Changes in the sedimentation coefficient promoted by the bisubstrate analogue N-(phosphonacetyl)-L-aspartate. Biochemistry 16:5077-5083, 1977.
10. Ladner, J.E., Kitchell, J.P., Honzatko, R.B., Ke, H.M., Volz, K.W., Kalb (Gilboa), A.J., Ladner, R.C., Lipscomb, W.N. Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-Å resolution study. Proc. Natl. Acad. Sci. USA 79:3125-3128, 1982.
11. Ke, H.-M., Lipscomb, W.N., Cho, Y., Honzatko, R.B. Complex of N-phosphonacetyl-L-aspartate with aspartate transcarbamoylase: X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms. J. Mol. Biol. 204:725-747, 1988.
12. Stevens, R.C., Chook, Y.M., Cho, C.Y., Lipscomb, W.N., Kantrowitz, E.R. Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesis. Protein Eng. 4:391-408, 1991.
13. Monaco, H.L., Crawford, J.L., Lipscomb, W.N. Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate. Proc. Natl. Acad. Sci. USA 75:5276-5280, 1978.
14. Moody, M.F., Vachette, P., Foote, A.M. Changes in the X-ray solution scattering of aspartate transcarbamoylase following the allosteric transition. J. Mol. Biol. 133:517-532, 1979.
15. Altman, R.B., Ladner, J.E., Lipscomb, W.N. Quaternary structural changes in aspartate carbamoyl transferase EC 2.1.3.2 of Escherichia coli at pH 8.3 and pH 5.8. Biochem Biophys. Res. Commun. 108:592-595, 1982.
16. Svergun, D.I., Barberato, C., Koch, M.H.J. CRYSOL: A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28:768-773, 1995.
17. Fetler, L., Tauc, P., Hervé, G., Moody, M.F., Vachette, P. X-ray scattering titration of quaternary structure transition of aspartate transcarbamylase with a bisubstrate analogue: Influence of nucleotide effectors. J. Mol. Biol. 251: 243-255, 1995.
18. Guinier, A., Fournet, G. "Small-Angle Scattering of X-rays." New-York: Wiley, 1955.
19. Jones, T.A., Zou, J.-Y., Cowan, S.W., Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47:110-119, 1991.
20. Krause, K.L., Volz, K.W., Lipscomb, W.N. 2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate. J. Mol. Biol. 193:527-553, 1987.
21. Gouaux, J.E., Lipscomb, W.N. Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-Å resolution and neutral pH. Biochemistry 29:389-402, 1990.
22. Gouaux, J.E., Lipscomb, W.N. Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase. Proc. Natl. Acad. Sci. USA 85:4205-4208, 1988.
23. Tsuruta, H., Vachette, P., Sano, T., Moody, M.F., Amemiya, Y., Wakabayashi, K., Kihara, H. Kinetics of the quaternary structure change of aspartate transcarbamylase triggered by succinate, a competitive inhibitor. Biochemistry 33:10007-10012, 1994.
24. Fermi, G., Perutz, M.F., Shaanan, B., Fourme, R. The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J. Mol. Biol. 175:159-174, 1984.
25. Shaanan, B. Structure of human oxyhaemoglobin at 2.1Å resolution. J. Mol. Biol. 171:31-59, 1983.
26. Smith, F.R., Lattman, E.E., Carter, C.W., Jr. The mutation b99 Asp-Tyr stabilizes Y: A new, composite quaternary state of human hemoglobin. Proteins 10:81-91, 1991.
27. Janin, J., Wodak, S.J. The quaternary structure of carbonmonoxy hemoglobin Ypsilanti. Proteins 15:1-4, 1993.
28. Silva, M.M., Rogers, P.H., Arnone, A. A third quaternary structure of human hemoglobin A at 1.7Å resolution. J. Biol. Chem. 267:17248-17256, 1992.
29. Srinivasan, R., Rose, G.D. The T-to-R transformation in hemoglobin: A reevaluation. Proc. Natl. Acad. Sci. USA 91:11113-11117, 1994.