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Volumn 61, Issue 1, 2005, Pages 209-212

The X-ray crystal structure of PA3566 from Pseudomonas aureginosa at 1.8 Å resolution

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; BACTERIAL PROTEIN; FERREDOXIN; PA3566 PROTEIN; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 24344467831     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20503     Document Type: Article
Times cited : (4)

References (22)
  • 1
    • 2942733563 scopus 로고    scopus 로고
    • New knowledge from old: In silico discovery of novel protein domains in Streptomyces coelicolor
    • Yeats C, Bentley S, Bateman A. New knowledge from old: in silico discovery of novel protein domains in Streptomyces coelicolor. BMC Microbiol 2003;3:3.
    • (2003) BMC Microbiol , vol.3 , pp. 3
    • Yeats, C.1    Bentley, S.2    Bateman, A.3
  • 2
    • 0026656038 scopus 로고
    • Crystal structure at 1.7 a of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target
    • Hegde RS, Grossman SR, Laimins LA, Sigler PB. Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target. Nature 1992;359:505-512.
    • (1992) Nature , vol.359 , pp. 505-512
    • Hegde, R.S.1    Grossman, S.R.2    Laimins, L.A.3    Sigler, P.B.4
  • 3
    • 0024961686 scopus 로고
    • Crystal structure of muconolactone isomerase at 3.3 a resolution
    • Katti SK, Katz BA, Wyckoff HW. Crystal structure of muconolactone isomerase at 3.3 A resolution. J Mol Biol 1989;205:557-571.
    • (1989) J Mol Biol , vol.205 , pp. 557-571
    • Katti, S.K.1    Katz, B.A.2    Wyckoff, H.W.3
  • 4
    • 0037439266 scopus 로고    scopus 로고
    • The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis
    • Sciara G, et al. The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis. EMBO J 2003;22:205-215.
    • (2003) EMBO J , vol.22 , pp. 205-215
    • Sciara, G.1
  • 5
    • 0027918137 scopus 로고
    • α plus β folds revisited: Some favoured motifs
    • Orengo CA, Thornton JM. α plus β folds revisited: some favoured motifs. Structure 1993;1:105-120.
    • (1993) Structure , vol.1 , pp. 105-120
    • Orengo, C.A.1    Thornton, J.M.2
  • 6
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sanders C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sanders, C.2
  • 7
    • 0028566270 scopus 로고
    • A revised set of potentials for β-turn formation in proteins
    • Hutchinson EG, Thornton JM. A revised set of potentials for β-turn formation in proteins. Protein Sci 1994;3:2207-2216.
    • (1994) Protein Sci , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 8
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions derived from structural studies
    • Jones S, Thornton JM. Principles of protein-protein interactions derived from structural studies. Proc Natl Acad Sci USA 1996;93: 13-20.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 9
    • 0030858888 scopus 로고    scopus 로고
    • Identification of a monooxygenase from Streptomyces coelicolor A3(2) involved in the biosynthesis of actinorhodin: Purification and characterization of the recombinant enzyme
    • Kendrew SG, Hopwood DA, Marsh ENG. Identification of a monooxygenase from Streptomyces coelicolor A3(2) involved in the biosynthesis of actinorhodin: purification and characterization of the recombinant enzyme. J Bacteriol 1997;179:4305-4310.
    • (1997) J Bacteriol , vol.179 , pp. 4305-4310
    • Kendrew, S.G.1    Hopwood, D.A.2    Marsh, E.N.G.3
  • 10
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • Berman HM, et al. The Protein Data Bank. Nucleic Acids Res 2000;28:235-242.
    • (2000) Nucleic Acids Res , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 11
  • 12
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt GJ, Jones TA. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr 1994;D50:178-185.
    • (1994) Acta Crystallogr , vol.D50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 13
    • 0035190121 scopus 로고    scopus 로고
    • Structure of Thermotoga maritima stationary phase survival protein SurE: A novel acid phosphatase
    • Zhang RG, et al. Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase. Structure (Camb.) 2001;9:1095-1106.
    • (2001) Structure (Camb.) , vol.9 , pp. 1095-1106
    • Zhang, R.G.1
  • 14
    • 0033213109 scopus 로고    scopus 로고
    • MAD data collection-current rrends
    • Walsh MA, et al. MAD data collection-current rrends. Acta Crystallogr 1999;D55:1726-1732.
    • (1999) Acta Crystallogr , vol.D55 , pp. 1726-1732
    • Walsh, M.A.1
  • 15
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. Solvent content of protein crystals. J Mol Biol 1968;33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, et al. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr 1991;A47:110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1
  • 20
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • CCP4. The CCP4 Suite: programs for protein crystallography. Acta Crystallogr D 1994;D50:760-763.
    • (1994) Acta Crystallogr D , vol.D50 , pp. 760-763
  • 21
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, et al. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999;15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.