The crystal structures of the complexes between bovine β-trypsin and ten P1 variants of BPTI

Journal of Molecular Biology

Volumn 287, Issue 5, 1999, Pages 923-942

  Helland, Ronny ^a   Otlewski, Jacek ^b   Sundheim, Ottar ^a   Dadlez, Michal ^c   Smalås, Arne O ^a  

^a UNIVERSITY OF TROMSØ   (Norway)

^b UNIVERSITY OF WROC AW   (Poland)

^c INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

Author keywords

Bovine pancreatic trypsin inhibitor; Non cognate binding; Protein protein interaction; Serine proteinase; Trypsin

Indexed keywords

APROTININ; ASPARTIC ACID; GLUTAMIC ACID; GLUTAMINE; GLYCINE; HISTIDINE; LYSINE; METHIONINE; PHENYLALANINE; SERINE PROTEINASE; THREONINE; TRYPSIN; TRYPTOPHAN; WATER;

ARTICLE; BINDING SITE; CATTLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HYDROGEN BOND; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; TEMPERATURE; X RAY CRYSTALLOGRAPHY;

EID: 0033574398     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2654     Document Type: Article

References (40)

1. Alber T., Sun D. P., Wilson K., Wozniak J. A., Cook S. P., Matthews B. W. Contributions of hydrogen-bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature. 330:1987;41-46.
2. Apostoluk W., Otlewski J. Variability of the canonical loop conformations in serine proteinases inhibitors and other proteins. Proteins: Struct. Funct. Genet. 32:1998;459-474.
3. Bartunik H. D., Summers L. J., Bartsch H. H. Crystal structure of bovine beta-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density. Active site geometry, ion pairs and solvent structure. J. Mol. Biol. 210:1989;813-828.
4. Bode W., Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204:1992;433-451.
5. Brünger A. T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-475.
6. Castro M. J., Anderson S. Alanine point-mutations in the reactive region of bovine pancreatic trypsin inhibitor: effects on the kinetics and thermodynamics of binding to beta-trypsin and alpha-chymotrypsin. Biochemistry. 35:1996;11435-11446.
7. Chen Z., Bode W. Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. Crystallization, Patterson search, structure determination, refinement, structure and comparison with its components and with the bovine trypsin-pancreatic trypsin inhibitor complex. J. Mol. Biol. 164:1983;283-311.
8. Acta Crystallog. sect. D. 50:1994;760-763.
9. Deisenhofer J., Steigemann W. Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 Å resolution. Acta Crystallog. sect. B. 31:1975;238-250.
10. Eisenberg D., McLachlan A. D. Solvation energy in protein folding and binding. Nature. 319:1986;199-203.
11. Esnouf R. M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15:1997;133-138.
12. Hedstrom L., Szilagyi L., Rutter W. J. Converting trypsin to chymotrypsin: the role of surface loops. Science. 255:1992;1249-1253.
13. Helland R., Leiros I., Berglund G. I., Willassen N. P., Smalås A. O. The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor. Eur. J. Biochem. 256:1998;317-324.
14. Huang K., Lu W., Anderson S., Laskowski M. Jr, James M. N. Water molecules participate in proteinase-inhibitor interactions: crystal structures of Leu18, Ala18, and Gly18 variants of turkey ovomucoid inhibitor third domain complexed with Streptomyces griseus proteinase B. Protein Sci. 4:1995;1985-1997.
15. Huber R., Kukla D., Bode W., Schwager P., Bartels K., Deisenhofer J., Steigemann W. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 Å resolution. J. Mol. Biol. 89:1974;73-101.
16. Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
17. Kleywegt G. J., Brunger A. T. Checking your imagination: applications of the free R value. Structure. 4:1996;897-904.
18. Kraulis P. J. MOLSCRIPT: a program to produce both detailed and scematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
19. Krokoszynska I., Dadlez M., Otlewski J. Structure of single-disulfide variants of bovine pancreatic trypsin inhibitor (BPTI) as probed by their binding to bovine beta-trypsin. J. Mol. Biol. 275:1998;503-513.
20. Laskowski M. Jr, Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49:1980;593-626.
21. 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. Crystallog. 26:1993;283-291.
22. Lu W., Apostol I., Qasim M. A., Warne N., Wynn R., Zhang W. L., Anderson S., Chiang Y. W., Ogin E., Rothberg I., Ryan K., Laskowski M. Jr. Binding of amino acid side-chains to S1 cavities of serine proteinases. J. Mol. Biol. 266:1997;441-461.
23. Luzatti P. V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810.
24. Malikayil J. A., Burkhart J. P., Schreuder H. A., Broersma R. J. Jr, Tardif C., Kutcher L. W. R., Mehdi S., Schatzman G. L., Neises B., Peet N. P. Molecular design and characterization of an alpha-thrombin inhibitor containing a novel P1 moiety. Biochemistry. 36:1997;1034-1040.
25. Marquart M., Walter J., Diesenhofer J., Bode W., Huber R. The geometry of the reactive site and peptide groups in trypsin, trypsinogen and its complexes with inhibitors. Acta Crystallog. sect. B. 39:1983;480-490.
26. McGrath M. E., Erpel T., Bystroff C., Fletterick R. J. Macromolecular chelation as an improved mechanism of protease inhibition: Structure of the ecotin-trypsin complex. EMBO J. 13:1994;1502-1507.
27. McGrath M. E., Gillmor S. A., Fletterick R. J. Ecotin: lessons on survival in a protease-filled world. Protein Sci. 4:1995;141-148.
28. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in ocillation mode. Methods Enzymol. 276:1997;307-326.
29. Perona J. J., Craik C. S. Structural basis of substrate specificity in the serine proteases. Protein Sci. 4:1995;337-360.
30. Perona J. J., Tsu C. A., Craik C. S., Fletterick R. J. Crystal structures of rat anionic trypsin complexed with the protein inhibitors APPI and BPTI. J. Mol. Biol. 230:1993;919-933.
31. Perona J. J., Tsu C. A., Craik C. S., Fletterick R. J. Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix. Biochemistry. 36:1997;5381-5392.
32. Qasim M. A., Ganz P. J., Saunders C. W., Bateman K. S., James M. N., Laskowski M. Jr. Interscaffolding additivity. Association of P1 variants of eglin c and of turkey ovomucoid third domain with serine proteinases. Biochemistry. 36:1997;1598-1607.
33. Ramachandran G. N., Sasisekharan V. Conformation of polypeptides and proteins. Advan. Protein Chem. 23:1968;283-438.
34. Read R. J., James M. N. Introduction to protein inhibitors: X-ray crystallography. Barrett A. J., Salvesen G. Protease Inhibitors. 1986;301-336 Elsevier Science Publishers, Amsterdam.
35. Ruhlmann A., Kukla D., Schwager P., Bartels K., Huber R. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region. J. Mol. Biol. 77:1973;417-436.
36. Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:1967;157-162.
37. Scheidig A. J., Hynes T. R., Pelletier L. A., Wells J. A., Kossiakoff A. A. Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): engineering of inhibitors with altered specificities. Protein Sci. 6:1997;1806-1824.
38. van de Locht A., Lamba D., Bauer M., Huber R., Friedrich T., Kroger B., Hoffken W., Bode W. Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J. 14:1995;5149-5157.
39. van de Locht A., Bode W., Huber R., Le Bonniec B. F., Stone S. R., Esmon C. T., Stubbs M. T. The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin. EMBO J. 16:1997;2977-2984.
40. Wei A. Z., Mayr I., Bode W. The refined 2.3 Å crystal structure of human leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor. FEBS Letters. 234:1988;367-373.