Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: Evidence for decreased mobility of loops upon complexation

Journal of Molecular Biology

Volumn 271, Issue 2, 1997, Pages 258-265

  Edwards, Karen J ^a   Ollis, David L ^a   Dixon, Nicholas E ^a  

^a AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

Author keywords

Crystal structure; Cyclophilin; Peptidyl prolyl isomerase

Indexed keywords

ANILIDE; PROTEINASE;

ARTICLE; COMPARATIVE STUDY; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; R FACTOR;

ESCHERICHIA COLI;

EID: 0031571592     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1151     Document Type: Article

References (32)

1. Brünger A. T. X-PLOR Version 3.1. A System for X-ray Crystallography and NMR. 1992;Yale University, Connecticut.
2. 15. Biochemistry. 33:1994;4093-4100.
3. Clubb R. T., Ferguson S. B., Walsh C. T., Wagner G. Three-dimensional solution structure ofEscherichia coli. Biochemistry. 33:1994;2761-2772.
4. Compton L. A., Davis J. M., Macdonald J. R., Bächinger H. P. Structural and functional characterization ofEscherichia colicis-trans. Eur. J. Biochem. 206:1992;927-934.
5. Fejzo J., Etzkorn F. A., Clubb R. T., Shi Y., Walsh C. T., Wagner G. The mutantEscherichia coli. Biochemistry. 33:1994;5711-5720.
6. Fischer G., Witman-Liebold B., Lang K., Kiefhaber T., Schmid F. X. Cyclophilin and peptidyl-prolylcis-trans. Nature. 337:1989;476-478.
7. Galat A. Peptidylprolinecis-trans. Eur. J. Biochem. 216:1993;689-707.
8. Hayano T., Takahashi N., Kato S., Maki N., Suzuki M. Two distinct forms of peptidylprolyl-cis-transEscherichia coli. Biochemistry. 30:1991;3041-3048.
9. Kabsh W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
10. Kallen J., Walkinshaw M. D. The X-ray structure of a tetrapeptide bound to the active site of human cyclophilin A. FEBS Letters. 300:1992;286-290.
11. Ke H. Similarities and differences between human cyclophilin A and other β-barrel structures. J. Mol. Biol. 228:1992;539-550.
12. Ke H., Zydowsky L. D., Liu J., Walsh C. T. Crystal structure of recombinant human T-cell cyclophilin A at 2.5 Å resolution. Proc. Natl Acad. Sci. USA. 88:1991;9483-9487.
13. Ke H., Mayrose D., Cao W. Crystal structure of cyclophilin A complexed with substrate Ala-Pro suggests a solvent-assisted mechanism ofcis-trans. Proc. Natl Acad. Sci. USA. 90:1993;3324-3328.
14. Ke H., Mayrose D., Belshaw P. J., Alberg D. G., Schreiber S. L., Chang Z. Y., Etzkorn F. A., Ho S., Walsh C. T. Crystal structures of cyclophilin A complexed with cyclosporin A andN. Structure. 2:1994;33-44.
15. Kern G., Kern D., Schmid F. X., Fischer G. Reassessment of the putative chaperone function of prolyl-cistrans. FEBS Letters. 348:1994;145-148.
16. Konno M., Ito M., Hayano T., Takahashi N. The substrate-binding site inEscherichia colicistrans. J. Mol. Biol. 256:1996;897-908.
17. Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of proteins. J. Appl. Crystallog. 24:1991;946-950.
18. 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. 6:1993;283-291.
19. Liu J., Walsh C. T. Peptidyl-prolylcis-transEscherichia coli. Proc. Natl Acad. Sci. USA. 87:1990;4028-4032.
20. Liu J., Chen C.-M., Walsh C. T. Human andEscherichia coli. Biochemistry. 30:1991;2306-2310.
21. Love C. A., Lilley P. E., Dixon N. E. Stable high-copy-number bacteriophage λ promoter vectors for overproduction of proteins inEscherichia coli. Gene. 176:1996;49-53.
22. Matthews B. W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
23. Mikol V., Kallen J., Pflügl G., Walkinshaw M. D. X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 Å resolution. J. Mol. Biol. 234:1993;1119-1130.
24. Milan D., Griffith J., Su M., Price E. R., McKeon F. The latch region of calcineurin B is involved in both immunosuppressant-immunophilin complex docking and phosphatase activation. Cell. 79:1994;437-447.
25. Pflügl G. M., Kallen J., Jansonius J. N., Walkinshaw M. D. The molecular replacement solution and X-ray refinement to 2.8 Å of a decameric complex of human cyclophilin A with the immunosuppressive drug cyclosporin A. J. Mol. Biol. 244:1994;385-409.
26. Ramachandran G. N., Sasisekharan V. Conformation of polypeptides and proteins. Advan. Protein Chem. 23:1968;283-437.
27. Schreiber S. L., Crabtree G. R. The mechanism of action of cyclosporin A and FK506. Immunol. Today. 13:1992;136-142.
28. Spitzfaden C., Weber H.-P., Braun W., Kallen J., Wider G., Widmer H., Walkinshaw M. D., Wüthrich K. Cyclosporin A-cyclophilin complex formation: a model based on X-ray and NMR data. FEBS Letters. 300:1992;291-300.
29. Teague S. Lessons from molecular matchmakers. Nature Struct. Biol. 2:1995;360-361.
30. Thériault Y., Logan T. M., Meadows R., Yu L., Olejniczak E. T., Holzman T. F., Simmer R. L., Fesik S. W. Solution structure of the cyclosporin A/cyclophilin complex by NMR. Nature. 361:1993;88-91.
31. Trandinh C. C., Pao G. M., Saier M. H. Jr. Structural and evolutionary relationships among the immunophilins: two ubiquitous families of peptidyl-prolylcis-trans. FASEB J. 6:1992;3410-3420.
32. Walsh C. T., Zydowsky L. D., McKeon F. D. Cyclosporin A, the cyclophilin class of peptidylprolyl isomerases, and blockade of T cell signal transduction. J. Biol. Chem. 267:1992;13115-13118.