X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme

Nature Structural Biology

Volumn 3, Issue 3, 1996, Pages 284-289

  Pares, S ^a   Mouz, N ^a   Petillot Y ^a   Hakenbeck, R ^b   Dideberg, O ^a  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b MAX PLANCK INSTITUTE FOR MOLECULAR GENETICS   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; PENICILLIN BINDING PROTEIN; PENICILLIN DERIVATIVE;

ARTICLE; BACTERIUM CULTURE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME STRUCTURE; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; STREPTOCOCCUS PNEUMONIAE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CARRIER PROTEINS; CELL MEMBRANE; CRYSTALLOGRAPHY, X-RAY; HEXOSYLTRANSFERASES; MEMBRANE PROTEINS; METHIONINE; MODELS, MOLECULAR; MODELS, STRUCTURAL; MOLECULAR SEQUENCE DATA; MURAMOYLPENTAPEPTIDE CARBOXYPEPTIDASE; PENICILLIN-BINDING PROTEINS; PENICILLINS; PEPTIDYL TRANSFERASES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; STREPTOCOCCUS PNEUMONIAE;

EID: 0029988098     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0396-284     Document Type: Article

References (24)

1. Hakenbeck, R., Briese, T. & Ellerbrok, H. Antibodies against the benzylpenicilloyl moiety as a probe for penicillin-binding proteins. Eur. J. Biochem. 157, 101-106 (1986).
2. Hakenbeck, R. & Kohiyama, M. Purification of penicillin-binding protein 3 from Streptococcus pneumoniae. Eur. J. Biochem. 127, 231-236 (1982).
3. Waxman, D.J. & Strominger, J.L. Penicillin-binding proteins and the mechanism of action of β-lactam antibiotics. Annu. Rev. Biochem. 52, 825-865 (1983).
4. Matsuhashi, M. in New Comprehensive Biochemistry. Bacterial Cell Wall Vol. 27, (eds J.-M. Ghuysen & R. Hakenbeck) 55-71 (Elsevier Science Publishers, Amsterdam 1994).
5. Spratt, E.G. Resistance to antibiotics mediated by target alterations. Science 264, 388-393 (1994).
6. Laible, G., Spratt, B.G. & Hakenbeck, R. Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae. Mol. Microbiol. 5, 1993-2002 (1991).
7. Laible, G. & Hakenbeck, R. Penicillin-binding proteins in β-lactam-resistant laboratory mutants of Streptococcus pneumoniae. Mol. Microbiol. 1, 355-363 (1987).
8. Charlier, P. et al. Crystallization of a genetically engineered water-soluble primary penicillin target enzyme. The high molecular mass PBP2x of Streptococcus pneumoniae. J. Mol. Biol. 232, 1007-1009 (1993).
9. Lobkovsky, E. et al. Evolution of an enzyme activity: Crystallographic structure at 2- Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc. Natl. Acad. Sci. USA 90, 11257-11261 (1993).
10. Kelly, J.A. & Kuzin, A.P. The refined Crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 Å resolution. J. Mol. Biol. 254, 223-236 (1995).
11. Jamin, M., Damblon, C., Miller, S., Hakenbeck, R. & Frère, J.-M. Penicillin-binding protein 2x of Streptococcus pneumoniae: enzymic activities and interactions with β-lactams. Biochem. J. 292, 735-741 (1993).
12. Adachi, H., Ohta, T. & Matsuzawa, H. Site-directed mutants, at position 166, of RTEM-1 β-lactamase that form a stable acyl-enzyme intermediate with penicillin. J. Biol. Chem. 266, 3185-3191 (1991).
13. Bustos, J.F., Chait, B.T. & Tomasz, A. Structure of the peptide network of pneumococcal peptidoglycan. J. Biol. Chem. 262, 15400-15405 (1987).
14. Kuroki, R., Weaver, L.H. & Matthews, B.W. A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme. Science 262, 2030-2033 (1993).
15. Messerschmidt, A. & Pflugrath, J.W. Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in Macromolecular Crystallography. J. Appl. Crystallogr. 20, 306-315 (1987).
16. Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 (1993).
17. CCP4, Collaborative Computing Project No. 4, Acta Crystallogr. D50, 760-763 (1993).
18. Otwinowski, W. Isomorphous Replacement and Anomalous Scattering, Proceedings of the CCP4 Study Weekend, (eds Wolf, W., Evans, P.R. & Leslie, A.G.W.) 80-86 (SERC Daresbury Laboratory, Warrington, 1991).
19. Zhang, K.Y.J. & Main, P. The use of Sayre's equation with solvent flattening and histogram matching for phase extension and refinement of protein structures. Acta Crystallogr. A46, 377-381 (1990).
20. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119 (1991).
21. Read, R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A42, 140-149 (1986).
22. Brünger, A.T. A system for X-ray Crystallography and NMR. X-PLOR Version 3.0. Yale Univ. Press, New Haven (1992).
23. Kraulis, P.J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
24. Nicholls, A., Sharp, K.A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-286 (1991).