Structure of the cathelicidin motif of protegrin-3 precursor: Structural insights into the activation mechanism of an antimicrobial protein

Structure

Volumn 10, Issue 10, 2002, Pages 1363-1370

  Sanchez, Jean Frédéric ^a   Hoh, François ^a   Strub, Marie Paule ^a   Aumelas, André ^a   Dumas, Christian ^a  

^a CENTRE DE BIOCHIMIE STRUCTURALE   (France)

Author keywords

Antimicrobial peptides; Cathelicidin; Domain swapping; Protegrin; Selenocysteine; X ray structure

Indexed keywords

CATHELICIDIN; CYSTATIN; DIMER; MONOMER; PROTEGRIN; PROTEGRIN 3; PROTEIN PRECURSOR; SELENOCYSTEINE; UNCLASSIFIED DRUG;

ANTIMICROBIAL ACTIVITY; ARTICLE; CHEMICAL LABELING; CRYSTAL STRUCTURE; DISPERSION; DRUG MECHANISM; METHODOLOGY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FAMILY; PROTEIN MOTIF; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; X RAY ANALYSIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN FOLDING; PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

MAMMALIA;

EID: 0036772907     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00859-6     Document Type: Article

References (41)

1. Lehrer R.I., Ganz T. Cathelicidins. a family of endogenous antimicrobial peptides Curr. Opin. Hematol. 9:2002;18-22.
2. Gennaro R., Zanetti M. Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers. 55:2000;31-49.
3. Ramanathan B., Davis E.G., Ross C.R., Blecha F. Cathelicidins. microbicidal activity, mechanisms of action, and roles in innate immunity Microbes Infect. 4:2002;361-372.
4. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature. 415:2002;389-395.
5. Nizet V., Ohtake T., Lauth X., Trowbridge J., Rudisill J., Dorschner R.A., Pestonjamasp V., Piraino J., Huttner K., Gallo R.L. Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature. 414:2001;454-457.
6. Müller S., Senn H., Gsell B., Vetter W., Baron C., Böck A. The formation of diselenide bridges in proteins by incorporation of selenocysteine residues. biosynthesis and characterization of (Se)2-thioredoxin Biochemistry. 33:1994;3404-3412.
7. Hendrickson W.A., Horton J.R., LeMaster D.M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD). a vehicle for direct determination of three-dimensional structure EMBO J. 9:1990;1665-1672.
8. Staniforth R.A., Giannini S., Higgins L.D., Conroy M.J., Hounslow A.M., Jerala R., Craven C.J., Waltho J.P. Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily. EMBO J. 20:2001;4774-4781.
9. Newcomer M.E. Protein folding and three-dimensional domain swapping. a strained relationship? Curr. Opin. Struct. Biol. 12:2002;48-53.
10. Liu Y., Eisenberg D. 3D domain swapping. as domains continue to swap Protein Sci. 11:2002;1285-1299.
11. Janowski R., Kozak M., Jankowska E., Grzonka Z., Grubb A., Abrahamson M., Jaskolski M. Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping. Nat. Struct. Biol. 8:2001;316-320.
12. Knaus K.J., Morillas M., Swietnicki W., Malone M., Surewicz W.K., Yee V.C. Crystal structure of the human prion protein reveals a mechanism for oligomerization. Nat. Struct. Biol. 8:2001;770-774.
13. Hendrickson W.A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science. 254:1991;51-58.
14. Pegoraro S., Fiori S., Cramer J., Rudolph-Bohner S., Moroder L. The disulfide-coupled folding pathway of apamin as derived from diselenide-quenched analogs and intermediates. Protein Sci. 8:1999;1605-1613.
15. Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:1993;123-138.
16. Bode W., Engh R., Musil D., Thiele U., Huber R., Karshikov A., Brzin J., Kos J., Turk V. The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7:1988;2593-2599.
17. Sanchez J.F., Wojcik F., Yang Y.S., Strub M.P., Strub J.M., Van Dorsselaer A., Martin M., Lehrer R., Ganz T., Chavanieu A.et al. Overexpression and structural study of the cathelicidin motif of the protegrin-3 precursor. Biochemistry. 41:2002;21-30.
18. Somoza J.R., Jiang F., Tong L., Kang C.H., Cho J.M., Kim S.H. Two crystal structures of a potently sweet protein. Natural monellin at. 2.75 Å resolution and single-chain monellin at 1.7 Å resolution. J. Mol. Biol. 234:1993;390-404.
19. Nagata K., Kudo N., Abe K., Arai S., Tanokura M. Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica. Biochemistry. 39:2000;14753-14760.
20. Martin J.R., Craven C.J., Jerala R., Kroon-Zitko L., Zerovnik E., Turk V., Waltho J.P. The three-dimensional solution structure of human stefin A. J. Mol. Biol. 246:1995;331-343.
21. Stubbs M.T., Laber B., Bode W., Huber R., Jerala R., Lenarcic B., Turk V. The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain. a novel type of proteinase inhibitor interaction EMBO J. 9:1990;1939-1947.
22. Murzin A.G. Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors. J. Mol. Biol. 230:1993;689-694.
23. Sanchez J.F., Hoh F., Strub M.P., Strub J.M., Van Dorsselaer A., Lehrer R., Ganz T., Chavanieu A., Calas B., Dumas C.et al. Expression, purification, crystallization and preliminary X-ray analysis of the cathelicidin motif of the protegrin-3 precursor. Acta Crystallogr. D. 57:2001;1677-1679.
24. O'Neill J.W., Kim D.E., Johnsen K., Baker D., Zhang K.Y. Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus. Structure. 9:2001;1017-1027.
25. Rousseau F., Schymkowitz J.W., Wilkinson H.R., Itzhaki L.S. Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues. Proc. Natl. Acad. Sci. USA. 98:2001;5596-5601.
26. Cole A.M., Shi J., Ceccarelli A., Kim Y.H., Park A., Ganz T. Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds. Blood. 97:2001;297-304.
27. Aumelas A., Mangoni M., Roumestand C., Chiche L., Despaux E., Grassy G., Calas B., Chavanieu A. Synthesis and solution structure of the antimicrobial peptide protegrin-1. Eur. J. Biochem. 237:1996;575-583.
28. Fahrner R.L., Dieckmann T., Harwig S.S., Lehrer R.I., Eisenberg D., Feigon J. Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes. Chem. Biol. 3:1996;543-550.
29. Lawrence M.C., Colman P.M. Shape complementarity at protein/protein interfaces. J. Mol. Biol. 234:1993;946-950.
30. Otwinowski Z., Minor W. Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-325.
31. Terwilliger T.C., Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr. D. 55:1999;849-861.
32. de la Fortelle E.D., Bricogne G. Maximum-likelihood heavy atom parameter refinement in the MIR and MAD methods. Methods Enzymol. 276:1997;472-492.
33. Abrahams J., Leslie A. Methods used in the structure determintion of bovine mitochondrial F1 ATPase. Acta Crystallogr. D. 52:1996;30-42.
34. Jones T.A., Kjeldgaard M. Electron-density map interpretation. Methods Enzymol. 277:1997;173-208.
35. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S.et al. Crystallography and NMR system. a new software suite for macromolecular structure determination Acta Crystallogr. D. 54:1998;905-921.
36. Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. Procheck. a program to check the stereochemistry quality of protein structures J. Appl. Crystallogr. 26:1993;283-291.
37. CCP4 Collaborative Computational Project Number 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
38. Engh R.A., Huber R. Accurate bond and angle parameters for x-ray protein structure refinement. Acta Crystallogr. A. 47:1991;392-400.
39. Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structure J. Appl. Crystallogr. 24:1991;946-950.
40. Merrit E.A., Bacon D.J. Raster3D:photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
41. Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296.