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Volumn 54, Issue 5, 2010, Pages 2167-2174

Crystal structure of the narrow-spectrum OXA-46 class D β-lactamase: Relationship between active-site lysine carbamylation and inhibition by polycarboxylates

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BETA LACTAMASE; LYSINE; OXA 46; SERINE; TARTARIC ACID; UNCLASSIFIED DRUG;

EID: 77951249585     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01517-09     Document Type: Article
Times cited : (34)

References (32)
  • 1
    • 66749100727 scopus 로고    scopus 로고
    • Discovery of novel lipophilic inhibitors of OXA-10 enzyme (class D β-lactamase) by screening amino analogs and homologs of citrate and isocitrate
    • Beck, J., L. Vercheval, C. Bebrone, A. Herteg-Fernea, P. Lassaux, and J. Marchand-Brynaert. 2009. Discovery of novel lipophilic inhibitors of OXA-10 enzyme (class D β-lactamase) by screening amino analogs and homologs of citrate and isocitrate. Bioorg. Med. Chem. Lett. 19:3593-3597.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 3593-3597
    • Beck, J.1    Vercheval, L.2    Bebrone, C.3    Herteg-Fernea, A.4    Lassaux, P.5    Marchand-Brynaert, J.6
  • 2
    • 34548558727 scopus 로고    scopus 로고
    • Crystallization of soluble proteins in vapor diffusion for X-ray crystallography
    • Benvenuti, M., and S. Mangani. 2007. Crystallization of soluble proteins in vapor diffusion for X-ray crystallography. Nat. Protoc. 2:1633-1651.
    • (2007) Nat. Protoc. , vol.2 , pp. 1633-1651
    • Benvenuti, M.1    Mangani, S.2
  • 3
    • 77951241824 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N4
    • Collaborative Computational Project, N4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 5
    • 0000144850 scopus 로고
    • The fast rotation function
    • M. J. Rossmann (ed.), Gordon & Breach, New York, NY
    • Crowther, R. A. 1972. The fast rotation function, p. 173-178. In M. J. Rossmann (ed.), The molecular replacement method. Gordon & Breach, New York, NY.
    • (1972) The Molecular Replacement Method , pp. 173-178
    • Crowther, R.A.1
  • 6
    • 0035831312 scopus 로고    scopus 로고
    • Evidence of dimerisation among class D β-lactamases: Kinetics of OXA-14 β-lactamase
    • Danel, F., J. M. Frere, and D. M. Livermore. 2001. Evidence of dimerisation among class D β-lactamases: kinetics of OXA-14 β-lactamase. Biochim. Biophys. Acta 1546:132-142.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 132-142
    • Danel, F.1    Frere, J.M.2    Livermore, D.M.3
  • 8
  • 11
    • 0034725405 scopus 로고    scopus 로고
    • The first structural and mechanistic insights for class D β-lactamases: Evidence for a novel catalytic process for turnover of β-lactam antibiotics
    • Golemi, D., L. Maveyraud, S. Vakulenko, S. Tranier, A. Ishiwata, L. P. Kotra, J. P. Samama, and S. Mobashery. 2000. The first structural and mechanistic insights for class D β-lactamases: evidence for a novel catalytic process for turnover of β-lactam antibiotics. J. Am. Chem. Soc. 122:6132-6133.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 6132-6133
    • Golemi, D.1    Maveyraud, L.2    Vakulenko, S.3    Tranier, S.4    Ishiwata, A.5    Kotra, L.P.6    Samama, J.P.7    Mobashery, S.8
  • 13
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. Macarthur, D. S. Moss, and J. M. Thornton. 1993. Procheck: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 14
    • 0002414103 scopus 로고
    • Molecular data processing
    • V. Moras, A. D. Podjarny, and J. P. Thierry (ed.), Oxford University Press, Oxford, England
    • Leslie, A. G. W. 1991. Molecular data processing, p. 50-61. In V. Moras, A. D. Podjarny, and J. P. Thierry (ed.), Crystallographic computing V. Oxford University Press, Oxford, England.
    • (1991) Crystallographic Computing V , pp. 50-61
    • Leslie, A.G.W.1
  • 15
    • 34447332502 scopus 로고    scopus 로고
    • Introduction: The challenge of multiresistance
    • Livermore, D. M. 2007. Introduction: the challenge of multiresistance. Int. J. Antimicrob. Agents 29(Suppl. 3):S1-S7.
    • (2007) Int. J. Antimicrob. Agents , vol.29 , Issue.SUPPL. 3
    • Livermore, D.M.1
  • 16
    • 0034476988 scopus 로고    scopus 로고
    • Insights into class D β-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa
    • Maveyraud, L., D. Golemi, L. P. Kotra, S. Tranier, S. Vakulenko, S. Mobashery, and J. P. Samama. 2000. Insights into class D β-lactamases are revealed by the crystal structure of the OXA10 enzyme from Pseudomonas aeruginosa. Structure 8:1289-1298.
    • (2000) Structure , vol.8 , pp. 1289-1298
    • Maveyraud, L.1    Golemi, D.2    Kotra, L.P.3    Tranier, S.4    Vakulenko, S.5    Mobashery, S.6    Samama, J.P.7
  • 18
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. 1999. XtalView/Xfit: a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 20
  • 23
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., R. Morris, and V. S. Lamzin. 1999. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6:458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 24
    • 0036091783 scopus 로고    scopus 로고
    • Acquired carbapenem-hydrolyzing β-lactamases and their genetic support
    • Poirel, L., and P. Nordmann. 2002. Acquired carbapenem-hydrolyzing β-lactamases and their genetic support. Curr. Pharm. Biotechnol. 3:117-127.
    • (2002) Curr. Pharm. Biotechnol. , vol.3 , pp. 117-127
    • Poirel, L.1    Nordmann, P.2
  • 26
    • 34547422759 scopus 로고    scopus 로고
    • Carbapenemases: The versatile β-lactamases
    • Queenan, A. M., and K. Bush. 2007. Carbapenemases: the versatile β-lactamases. Clin. Microbiol. Rev. 20:440-458.
    • (2007) Clin. Microbiol. Rev. , vol.20 , pp. 440-458
    • Queenan, A.M.1    Bush, K.2
  • 27
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetric unit
    • Rossmann, M. J., and D. M. Blow. 1962. The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallogr. 15:24-31.
    • (1962) Acta Crystallogr. , vol.15 , pp. 24-31
    • Rossmann, M.J.1    Blow, D.M.2
  • 28
    • 34248326126 scopus 로고    scopus 로고
    • Crystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysis
    • Santillana, E., A. Beceiro, G. Bou, and A. Romero. 2007. Crystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysis. Proc. Natl. Acad. Sci. U. S. A. 104:5354-5359.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 5354-5359
    • Santillana, E.1    Beceiro, A.2    Bou, G.3    Romero, A.4
  • 29
    • 0037216363 scopus 로고    scopus 로고
    • Comparison of β-lactamases of classes a and D: 1.5-Å crystallographic structure of the class D OXA-1 oxacillinase
    • Sun, T., M. Nukaga, K. Mayama, E. H. Braswell, and J. R. Knox. 2003. Comparison of β-lactamases of classes A and D: 1.5-Å crystallographic structure of the class D OXA-1 oxacillinase. Protein Sci. 12:82-91.
    • (2003) Protein Sci. , vol.12 , pp. 82-91
    • Sun, T.1    Nukaga, M.2    Mayama, K.3    Braswell, E.H.4    Knox, J.R.5
  • 30
    • 0032078747 scopus 로고    scopus 로고
    • A translation-function approach for heavy-atom location in macromolecular crystallography
    • Vagin, A., and A. Teplyakov. 1998. A translation-function approach for heavy-atom location in macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 54:400-402.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 400-402
    • Vagin, A.1    Teplyakov, A.2
  • 31
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin, A., and A. Teplyakov. 2000. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 56:1622-1624.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 32
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A., and A. Teplyakov. 1997. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.