Insights into biomolecular function from small-angle scattering

Current Opinion in Structural Biology

Volumn 7, Issue 5, 1997, Pages 702-708

  Trewhella, Jill ^a  

^a LOS ALAMOS NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME;

CONFORMATION; CONFORMATIONAL TRANSITION; INSTRUMENTATION; LIGHT SCATTERING; MACROMOLECULE; MOLECULAR BIOLOGY; MOLECULAR INTERACTION; NEUTRON SCATTERING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DNA INTERACTION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; REVIEW; TECHNIQUE; X RAY ANALYSIS;

EID: 0030736871     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80081-4     Document Type: Article

References (37)

1. Moore PB. Small-angle scattering techniques for the study of biological macromolecules and macromolecular aggregates. Methods Exp Phys. 2:1982;337-390.
2. Schoenborn BP, Knott RB. Neutrons in Biology, Basic Life Sciences. 64:1996;Plenum Press, New York/London, This book gives an excellent up-to-date overview of neutron scattering in biology. of special interest.
3. Hyer D. Advanced Neutron Sources 1988. Institute of Physics Conference Series. 1989;Institute of Physics, Bristol/New York. No 97.
4. Chance B, Deisenhofer J, Ebashi S, Goodhead DT, Helliwell JR, Huxley HE, Iizuka T, Kirz J, Mitsui T, Rubenstein E. Synchrotron Radiation in the Biosciences. 1994;Clarendon Press, Oxford.
5. Willumeit R, Burkhardt N, Diedrich G, Zhao J, Nierhaus KH, Stuhrmann HB. The in situ structure of ribosomal proteins from polarized neutron scattering. J Mol Struct. 383:1996;201-211.
6. Wadzack J, Burkhardt N, Jünemann R, Diedrich G, Nierhaus KH, Frank J, Penczek P, Meerwinck W, Schmitt M, Willumeit R, Stuhrmann HB. Direct localization of the tRNAs within the elongating ribosome by means of neutron scattering (proton-spin contrast-variation). J Mol Biol. 266:1997;343-356 This is paper describes the application of a new approach to neutron contrast variation that increases signal-to-noise compared with conventional H/D substitution methods. The application demonstrates this approach's power in locating relatively small components of large assemblies. of special interest.
7. Serdyuk IN, Zaccai G. The triple isotopic substitution method in small-angle neutron scattering: application to studying macromolecular complexes. J Mol Struct. 383:1996;197-200.
8. Shi L, Kataoka M, Fink AL. Conformational characterization of DnaK and its components by small-angle X-ray scattering. Biochemistry. 35:1996;3297-3308.
9. Spurlino JC, Lu G-Y, Quiocho FA. The 2-3 Å resolution structure of the maltose or maltodextran-binding protein, a primary receptor of bacterial active transport and chemotaxis. J Biol Chem. 266:1991;5202-5219.
10. Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextran binding protein involved in active transport and chemotaxis. Biochemistry. 31:1992;10657-10663.
11. Shilton BH, Flocco MM, Nilsson M, Mowbray SL. Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: the maltose-, glucose/galactose- and ribose-binding proteins. J Mol Biol. 264:1996;350-363.
12. Shilton BH, Shuman HA, Mowbray SL. Crystal structures and solution conformations of a dominant-negative mutant of Escherichia coli maltose-binding protein. J Mol Biol. 264:1996;364-376.
13. Olah GA, Trakhanov S, Trewhella J, Quiocho FA. Leucine/isoleucine/valine-binding protein contracts upon binding of ligand. J Biol Chem. 268:1993;16241-16247.
14. 2+-dependent domain reorientation. of outstanding interest.
15. Svergun DI, Barberato C, Koch MH, Fetler L, Vachette P. Large differences are observed between the crystal and solution quaternary structures of allosteric aspartate transcarbamoylase. Proteins. 27:1997;110-117 This paper demonstrates the importance of being able to evaluate the solution conformations of large oligomeric assemblies. The solution characterization of the distinct R and T states of this allosteric enzyme shows important differences from the crystal structure determination of the R state, which has implications for the allosteric mechanism. of outstanding interest.
16. Ke H-M, Lipscomb WN, Cho CY, Honzatko RB. Complex of N-phosphonacetyl-L-aspartate with aspartate transcarbamoylase: X-ray refinement, analysis and conformational changes and catalytic and allosteric mechanisms. J Mol Biol. 204:1988;725-747.
17. Trewhella J. Conformational flexibility in biochemical regulation. Sarma RH, Sarma MH. Structural Biology: The State of the Art. 1994;Adenine Press, Schenectady, NY.
18. Clore GM, Bax A, Ikura M, Gronenborn AM. Structure of calmodulin-target peptide complexes. Curr Opin Struct Biol. 3:1993;838-845.
19. Ikura M. Calcium binding and conformational response in EF-hand proteins. Trends Biochem Sci. 21:1996;14-17.
20. Krueger JK, Olah GA, Rokop SE, Zhi G, Stull JT, Trewhella J. Structures of calmodulin and a functional myosin light chain kinase in the activated complex: a neutron scattering study. Biochemistry. 36:1997;6017-6023 This paper reports the first structural view of calmodulin complexed with a catalytically active target enzyme. It demonstrates the power of neutron scattering using specific deuteration and contrast variation for studying biomolecular complexes in solution. of outstanding interest.
21. Kemp BE, Pearson RB, Guerriero V, Bagchi IC, Means AR. The calmodulin-binding domain of chicken smooth muscle myosin light-chain kinase contains a pseudosubstrate sequence. J Biol Chem. 262:1987;2542-2548.
22. 2+-troponin C-troponin I derived from small-angle scattering data: implications for regulation. Biochemistry. 33:1994;12800-12806.
23. Lemmon MA, Bu Z, Ladbury JE, Zhou M, Pinchasi D, Lax I, Engelman DM, Schlessigner J. Two EGF molecules contribute additively to stabilization of the EGFR dimer. EMBO J. 16:1997;281-294 This paper describes an elegant small-angle scattering study that gives insights into ligand-induced receptor oligomerization as an initial signaling event. of special interest.
24. Rodgers KK, Bu Z, Fleming KG, Schatz DG, Engelman DM, Coleman JE. A zinc-binding domain involved in the dimerization of RAG1. J Mol Biol. 260:1996;70-84.
25. Tuzikov FV, Zinoviev VV, Vavilin VI, Malygin EG. Application of the small-angle X-ray scattering technique for the study of two-step equilibrium-substrate interactions. Biopolymers. 38:1996;131-139.
26. Forstner M, Müller A, Stolz M, Wallimann T. The active site histidines of creatine kinase. A critical role of his 61 situated on a flexible loop. Protein Sci. 6:1997;331-339.
27. Chen L, Hodgson KO, Doniach S. A lysozyme folding intermediate revealed by solution X-ray scattering. J Mol Biol. 261:1996;658-671 This paper describes an approach to extracting information on structural intermediates from mixtures of native, unfolded, and structural intermediates, and provides novel insights into lysozyme unfolding. of outstanding interest.
28. Radford SE, Dobson CM, Evans PA. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:1992;302-307.
29. Smith CK, Bu Z, Anderson KS, Sturtevant JM, Engelman DM, Regan L. Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Sci. 5:1996;2009-2019 This paper describes differences in the effects of mutations on the native and chemically denatured states of a protein. Scattering is used to directly observe differences in the denatured ensemble with increasing concentrations of denaturant. of special interest.
30. Castellano AC, Barteri M, Bianconi A, Bruni F, Longa SD, Paolinelli C. Conformational changes involved in the switch from ovalbumin to S-ovalbumin. Z Naturforsch. 51c:1996;379-385.
31. Petrescu A, Receveur V, Calmettes P, Durand D, Desmadril M, Roux B, Smith JC. Small-angle neutron scattering by a strongly denatured protein: analysis using random polymer theory. Biophys J. 72:1997;335-342.
32. Eliezer D, Doniach S, Hodgson KO, Tsurata H. The radius of gyration of an apomyoglobin folding intermediates. Science. 270:1995;487-488.
33. Semisotnov GV, Kihara H, Kotova NV, Kimura K, Amemiya Y, Wakabayashi K, Serdyuk IN, Timchenko AA, Chiba K, Nikaido K, Ikura T, Kuwajima K. Protein globuralization during folding. A study by synchrotron small-angle X-ray scattering. J Mol Biol. 262:1996;559-574 This paper describes a novel method for extracting time-resolved information on the degree of protein compaction, which allows for more rapid measurements. of special interest.
34. Seeger PA, Rokop SE, Palmer PD, Henderson SJ, Hobart DE, Trewhella J. Neutron resonance scattering shows specific binding of plutonium to the calcium-binding sites of the protein calmodulin and yields precise distance information. J Am Chem Soc. 119:1997;5118-5125 This paper describes the first application of neutron resonance scattering as a structural biology tool. Advances in neutron spallation source development will significantly increase the potential for its application to biological macromolecules in solution by facilitating the use of a range of nuclei to label proteins for resonance scattering experiments. of special interest.
35. Ikura M, Clore GM, Gronenborn AM, Zhu G, Klee CB, Bax A. Solution structure of a calmodulin - target peptide complex by multidimensional NMR. Science. 256:1992;632-638.
36. Knighton DR, Zheng J, Ten Eyck LF, Ashford VA, Xuong N-H, Taylor SS, Sowadski JM. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase. Science. 253:1991;407-414.
37. Krueger JK, Padre RC, Stull JT. Intrasteric regulation of myosin light chain kinase. J Biol Chem. 270:1995;16848-16853.