Streptomyces griseus aminopeptidase: X-ray crystallographic structure at 1.75 Å resolution

Journal of Molecular Biology

Volumn 265, Issue 5, 1997, Pages 620-636

  Greenblatt, H M ^a   Almog, O ^a,d   Maras, B ^b   Spungin Bialik, A ^c   Barra, D ^b   Blumberg, S ^c   Shoham, G ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

^c TEL AVIV UNIVERSITY   (Israel)

^d Ctr of Advanced Res in Biotechnol   (United States)

Author keywords

Aminopeptidase; Anomalous scattering; Calcium activation; Crystal structure; Double zinc metalloproteinase

Indexed keywords

AMINOPEPTIDASE; ARGININE; CYTOSOL AMINOPEPTIDASE; GLUTAMIC ACID; GLYCINE; MERCURY; MICROBIAL ENZYME; PHOSPHATE; ZINC;

AEROMONAS; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; STREPTOMYCES GRISEUS; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY;

AEROMONAS; BOVINAE; STREPTOMYCES GRISEUS; VIBRIO PROTEOLYTICUS;

EID: 0031556952     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0729     Document Type: Article

References (40)

1. Allen M. P., Yamada A. H., Carpenter F. H. Kinetic parameters of metal substituted leucine aminopeptidase from bovine lens. Biochemistry. 22:1983;3778-3783.
2. Almog O., Greenblatt H. M., Spungin A., Ben-Meir D., Blumberg S., Shoham G. Crystallization and preliminary crystallographic analysis of Streptomyces griseus aminopeptidase. J. Mol. Biol. 22:1993;342-344.
3. Ben-Bassat A., Bauer K., Chang S.-Y., Myambo K., Boosman A., Chang S. Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure. J. Bacteriol. 169:1987;751-757.
4. Ben-Meir D., Blumberg S. Biologicals from Recombinant Microorganisms and Animal Cells: Production and Recovery. 1991;VCH, Weinheim.
5. Ben-Meir D., Spungin A., Ashkenazi R., Blumberg S. Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution. Eur. J. Biochem. 212:1993;107-112.
6. Brünger A. T. X-PLOR, Version 3.0. 1990;Yale University, New Haven.
7. Burley S. K., David P. R., Taylor A., Lipscomb W. N. Molecular structure of leucine aminopeptidase at 2.7 Å resolution. Proc. Natl Acad. Sci. USA. 87:1990;6878-6882.
8. Burley S. K., David P. R., Sweet R. M., Taylor A., Lipscomb W. N. Structure determination and refinement of bovine lens leucine aminopeptidase and its complex with bestatin. J. Mol. Biol. 224:1992;113-140.
9. CCP4: Collaborative Computational Project Number 4. The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
10. Chevrier B., Schalk C., D'Orchymont H., Rondeau J.-M., Moras D., Tarnus C. Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure. 2:1994;283-291.
11. Coleman J. E., Vallee B. L. Metallocarboxypeptidases: stability constants and enzymatic characteristics. J. Biol. Chem. 236:1961;2244-2249.
12. Cowtan K. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography. 31:1994;34-38.
13. Engh R. A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A. 47:1991;392-400.
14. Feinberg H., Greenblatt H. M., Shoham G. Binding and catalytic roles of the active site metal in zinc proteinases. J. Chem. Inf. Comput. Sci. 33:1993;501-516.
15. Feinberg H., Greenblatt H. M., Behar V., Gilon C., Cohen S., Bino A., Shoham G. Zinc-directed inhibitors for zinc proteinases. Acta Crystallog. sect. D. 51:1995;428-449.
16. Fujinaga M., Delbaere L. T. J., Brayer G. D., James M. N. G. Refined structure of α-lytic protease at 1.7 Å resolution. Analysis of hydrogen bonding and solvent structure. J. Mol. Biol. 183:1985;479-502.
17. Gomis-Rüth F. X., Kress L. F., Kellerman J., Mayr I., Lee X., Huber R., Bode W. Refined 2.0 Å X-ray crystal structure of the snake venom zinc-endopeptidase adamalysinII. J. Mol. Biol. 239:1994;513-544.
18. Indig F. E., Ben-Meir D., Spungin A., Blumberg S. Investigation of neutral endopeptidases (EC 3.4.24.11) and of neutral proteinases (EC 3.4.24.4) using a new sensitive two-stage enzymatic reaction. FEBS Letters. 255:1989;237-240.
19. Indig F. E., Benayahu D., Fried A., Wientroub S., Blumberg S. Neutral endopeptidisase (EC 3.4.24.11) is highly expressed on osteoblastic cells and other marrow stromal cell types. Biochem. Biophys. Res. Commun. 172:1990;620-626.
20. Kim H., Lipscomb W. N. Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by X-ray crystallography. Proc. Natl Acad. Sci. USA. 90:1993a;5006-5010.
21. Kim H., Lipscomb W. N. X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: formulation of a catalytic mechanism featuring a gem-diolate transition state. Biochemistry. 32:1993b;8465-8478.
22. 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;287-291.
23. Maras B., Greenblatt H. M., Shoham G., Spungin-Bialik A., Blumberg S., Barra D. Aminopeptidase from Streptomyces griseus: primary structure, and comparison with other zinc-containing aminopeptidases. Eur. J. Biochem. 236:1996;843-846.
24. Matthews B. M. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
25. Nagakawa S., Yamada T., Kato K., Nishimura O. Enzymatic cleavage of amino terminal methionine from recombinant human interleukin 2 and growth hormone by aminopeptidase M. Biotechnology. 5:1987;824-827.
26. Narahashi Y., Yanagita M. Studies on proteolytic enzymes (Pronase) of Streptomyces griseus K-1. Nature and properties of the proteolytic enzyme system. J. Biochem. (Tokyo). 62:1967;633-641.
27. Nishizawa M., Yasuhara T., Nakai T., Fujiki Y., Ohashi A. Molecular cloning of theaminopeptidase Y gene from Saccharomyces cerevisiae. J. Biol. Chem. 269:1994;13651-13655.
28. Otwinowski Z. Proceedings of the CCP4 Study Weekend. Wolf W., Evans P. R., Leslie A. G. W. 1991;Daresbury Laboratory, Daresbury.
29. Prescott J. M., Wagner F. W., Holmquist B., Vallee B. L. Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: non-identical, interacting metal-binding sites. Biochemistry. 32:1985;6493-6500.
30. Ramachandran G. N., Ramakrishnan C., Sasisekharan V. Stereochemistry of polypeptide chain configurations. J. Mol. Biol. 7:1963;95-99.
31. Rees D. C., Howard J. B., Chakrabarti P., Yeates T., Hsu B. T., Hardman K. D., Lipscomb W. N. Crystal structures of metallosubstituted carboxypeptidase. Zinc Enzymes. 1986;Birkhauser, Boston.
32. Roderick S. L., Matthews B. W. Structure of the cobalt-dependant methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Biochemistry. 32:1993;3907-3912.
33. Sack J. S. Chain; a crystallographic modeling program. J. Mol. Graphics. 6:1988;244-245.
34. Sato M., Yamamoto M., Imada K., Katsube Y., Tanaka N., Higashi T. High-speed data collection system for large unit cell crystals using an imaging plate as a detector. J. Appl. Crystallog. 25:1992;348-357.
35. Spungin A., Blumberg S. Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme. Eur. J. Biochem. 183:1989;471-477.
36. Sträter N., Lipscomb W. N. Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 Å resolution in a new crystal form. Biochemistry. 34:1995a;9200-9210.
37. Sträter N., Lipscomb W. N. Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem -diolate transition state analogue, by X-ray crystallography. Biochemistry. 34:1995b;14792-14800.
38. Tronrud D. E. Conjugate-direction minimization. An improved method for the refinement of macromolecules. Acta Crystallog. sect. A. 48:1992;912-916.
39. Vosbeck K. D., Chow K. F., Awad W. M., Jr. The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). J. Biol. Chem. 248:1973;6029-6034.
40. Yasuhara T., Nakai T., Ohashi A. Aminopeptidase Y, a new aminopeptidase from Saccharomyces cerevisiae. J. Biol. Chem. 269:1994;13644-13650.