Solution structure of marinostatin, a natural ester-linked protein protease inhibitor

Biochemistry

Volumn 44, Issue 7, 2005, Pages 2462-2468

  Kanaori, Kenji ^a   Kamei, Kaeko ^a   Taniguchi, Mai ^a   Koyama, Takao ^a   Yasui, Tomoharu ^a   Takano, Ryo ^a   Imada, Chiaki ^b   Tajima, Kunihiko ^a   Hara, Saburo ^a  

^a KYOTO INSTITUTE OF TECHNOLOGY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; DEUTERIUM; ESTERS; HYDROGEN; HYDROGEN BONDS; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTONS; PURIFICATION; SOLUTIONS; SYNTHESIS (CHEMICAL);

CARBONYL OXYGEN; ESTER LINKAGES; MARINOSTATIN; PROTEASE;

PROTEINS;

ARGININE; ASPARTIC ACID; CARBOXYL GROUP; CYSTEINE; DEUTERIUM; ESTER; HYDROGEN; HYDROXYL GROUP; MARINOSTATIN; PROLINE; PROTEINASE INHIBITOR; SERINE; THREONINE; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CONFORMATION; DISULFIDE BOND; ENZYME ACTIVE SITE; HYDROGEN BOND; MOLECULAR DYNAMICS; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS;

ATP-BINDING CASSETTE TRANSPORTERS; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DEUTERIUM EXCHANGE MEASUREMENT; DISULFIDES; ESTERS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEASE INHIBITORS; PROTEIN CONFORMATION; PROTEIN PRECURSORS; SERINE PROTEINASE INHIBITORS; SOLUTIONS; SUBTILISIN;

EID: 14044279911     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048034x     Document Type: Article

References (30)

1. Imada, C., Taga, N., and Maeda, M. (1985) Isolation and characterization of marine bacteria producing protease inhibitor, Bull. Jpn. Soc. Sci. Fish. 51, 805-810.
2. Imada, C., Hara, S., Maeda, M., and Simidu, U. (1986) Amino acid sequences of Marinostatins C-1 and C-2 from marine Alteromonas sp, Bull. Jpn. Soc. Sci. Fish. 52, 1455-1459.
3. Takano, R., Imada, C., Kainei, K., and Hara, S. (1991) The reactive site of marinostatin, a proteinase inhibitor from marine Alteromonas sp. B-10-31, J. Biochem. 110, 856-858.
4. Miyamoto, K., Tsujibo, H., Hikita, Y., Tanaka, K., Miyamoto, S., Hishimoto, M., Imada, C., Kamei, K., Hara, S., and Inamori, Y. (1998) Cloning and nucleotide sequence of the gene encoding a serine proteinase inhibitor named marinostatin from a marine bacterium, Alteromonas sp. strain B-10-31, Biosci. Biotechnol. Biochem. 62, 2446-2449.
5. Carrell, R. W. (1988) Alzheimer's disease. Enter a protease inhibitor, Nature 331, 478-479.
6. Gebhard, W., and Hochstrasser, K. (1986) Proteinase Inhibitors, Elsevier, Amsterdam.
7. Laskowski, M., and Kato, I. (1980) Protein inhibitors of proteinases, Annu. Rev. Biochem. 49, 593-626.
8. 1H NMR of the novel cyclic trypsin inhibitor SFTI-1 from sunflower seeds and an acyclic permutant, J. Mol. Biol. 311, 579-591.
9. Bode, W., Papamokos, E., and Musil, D. (1987) The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry, Eur. J. Biochem. 166, 673-692.
10. Bode, W., and Huber, R. (1992) Natural protein proteinase inhibitors and their interaction with proteinasesh, Eur. J. Biochem. 204, 433-451.
11. Green, N. M., and Work, E. (1953) Pancreatic trypsin inhibitor, Biochem. J. 54, 347-352.
12. Ranee, M., Sørensen, O. W., Bodenhausen, G., Wagner, G., Ernst, R. R., and Wüthrich, K. (1983) Improved spectral resolution in COSY proton NMR spectra of proteins via double quantum filtering, Biochem. Biophys. Res. Commun. 117, 479-485.
13. Bax, A., and Davis, D. G. (1985) MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy, J. Magn. Reson. 65, 355-360.
14. Jeener, J., Meier, B. H., Bachmann, P., and Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy, J. Chem. Phys. 71, 4546-4553.
15. Billeter, M., Braun, W., and Wüthrich, K. (1982) Sequential resonance assignments in protein proton nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single-crystal protein conformations, J. Mol. Biol. 155, 321-346.
16. Wüthrich, K., Billeter, M., and Braun, W. (1983) Pseudostructures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance, J. Mol. Biol. 169, 949-961.
17. Wüthrich, K., Billeter, M., and Braun, W. (1984) Polypeptide secondary structure determination by nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations, J. Mol. Biol. 180, 715-740.
18. Mer, G., Hietter, H., Kellenberger, C., Renatus, M., Luu, B., and Lefèvre, J.-F. (1996) Solution structure of PMP-C: A new fold in ht group of small serine proteinase inhibitors, J. Mol. Biol. 258, 158-171.
19. Wüthrich, K., Wider, G., Wagner, G., and Braun, W. (1982) Sequential resonance assignments as a basis for determination of spatial protein structures by high-resolution proton nuclear magnetic resonance, J. Mol. Biol. 155, 311-319.
20. Jackman, L. M., and Sternhell, S. (1969) Applications of Nuclear Magnetic Resonance Spectroscopy in Organic Chemistry, 2nd ed., Pergamon Press, Oxford.
21. Wishart, D. S., Sykes, B. D., and Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol. 222, 311-333.
22. Grathwohl, C., and Wüthrich, K. (1981) NMR studies of the rates of proline cis-trans isomerization in oligopeptides, Biopolymers 20, 2623-2633.
23. Brauer, A. B., Domingo, G. J., Cooke, R. M., Matthews, S. J., and Leatherbarrow, R. J. (2002) A conserved cis peptide bond is necessary for the activity of Bowman-Birk inhibitor protein, Biochemistry 41, 10608-10615.
24. Bai, Y., Milne, J. S., Mayne, L. M., and Englander, S. W. (1993) Primary structure effects on peptide group hydrogen exchange, Proteins: Struct., Funct., Genet. 17, 75-86.
25. McPhalen, C. A., Schnebli, H. P., and James, M. N. G. (1985) Crystal and molecular structure of the inhibitor eglin from leeches in complex with subtilisin Carlsberg, FEBS Lett. 188, 55-58.
26. McPhalen, C. A., Svendsen, I., Jonassen, I., and James, M. N. G. (1985) Crystal and molecular structure of the inhibitor CI-2 from barley seeds in complex with subtilisin novo, Proc. Natl. Acad. Sci. U.S.A. 82, 7242-7246.
27. Heinz, D. W., Priestle, J. P., Rahuel, J., Wilson, K. S., and Gratter, M. G. (1991) Refined crystal structure of subtilisin novo in complex with wild-type and two mutant eglins, J. Mol. Biol. 217, 353-371.
28. Takeuchi, Y., Satow, Y., Nakamura, K. T., and Mitsui, Y. (1991) Refined crystal structure of the complex of subtilisin BPN′ and Streptomyces subtilisin inhibitor at 1.8 Å resolution, J. Mol. Biol. 221, 309-325.
29. Fujinaga, M., Sielecki, A., Read, R., Ardelt, W., Laskowski, M. J., and James, M. (1987) Crystal and molecular structures of the complex of alpha-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 Å resolution, J. Mol. Biol. 195, 397-418.
30. Hiromi, K., Akasaka, K., Mitsui, Y., Tonomura, B., and Murao, S. (1985) Protein protease inhibitor - The case of Streptomyces subtilisin inhibitor (SSI), Elsevier, Amsterdam.