메뉴 건너뛰기




Volumn 408, Issue 2, 2011, Pages 356-361

Crystal structure and biophysical characterisation of Helicobacter pylori phosphopantetheine adenylyltransferase

Author keywords

Coenzyme A; Dinucleotide binding fold; Helicobacter pylori; Phosphopantetheine adenylyltransferase

Indexed keywords

BACTERIAL ENZYME; COENZYME A; PANTETHEINE PHOSPHATE ADENYLYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 79955650450     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.04.058     Document Type: Article
Times cited : (9)

References (32)
  • 2
    • 63849236851 scopus 로고    scopus 로고
    • Helicobacter pylori: phenotypes, genotypes and virulence genes
    • Proenca-Modena J.L., Acrani G.O., Brocchi M. Helicobacter pylori: phenotypes, genotypes and virulence genes. Future Microbiol. 2009, 4:223-240.
    • (2009) Future Microbiol. , vol.4 , pp. 223-240
    • Proenca-Modena, J.L.1    Acrani, G.O.2    Brocchi, M.3
  • 3
    • 33645740999 scopus 로고    scopus 로고
    • The pathogenesis of Helicobacter pylori -induced gastro-duodenal diseases
    • Atherton J.C. The pathogenesis of Helicobacter pylori -induced gastro-duodenal diseases. Annu. Rev. Pathol. 2006, 1:63-96.
    • (2006) Annu. Rev. Pathol. , vol.1 , pp. 63-96
    • Atherton, J.C.1
  • 5
    • 33748309036 scopus 로고    scopus 로고
    • Triple Standard quadruple and ampicillin-sulbactam-based quadruple therapies for H. pylori eradication: A comparative three-armed randomized clinical trial
    • Mirbagheri S.A., Hasibi M., Abouzari M., Rashidi A. Triple Standard quadruple and ampicillin-sulbactam-based quadruple therapies for H. pylori eradication: A comparative three-armed randomized clinical trial. World J. Gastroenterol. 2006, 12:4888-4891.
    • (2006) World J. Gastroenterol. , vol.12 , pp. 4888-4891
    • Mirbagheri, S.A.1    Hasibi, M.2    Abouzari, M.3    Rashidi, A.4
  • 6
    • 77749233911 scopus 로고    scopus 로고
    • A randomized controlled trial: efficacy and safety of azithromycin, ofloxacin, bismuth, and omeprazole compared with amoxicillin, clarithromycin, bismuth, and omeprazole as second-line therapy in patients with Helicobacter pylori infection
    • Minakari M., Jazi A.H.D., Shavakhi A., Moghareabed N., Fatahi F. A randomized controlled trial: efficacy and safety of azithromycin, ofloxacin, bismuth, and omeprazole compared with amoxicillin, clarithromycin, bismuth, and omeprazole as second-line therapy in patients with Helicobacter pylori infection. Helicobacter 2010, 15:154-159.
    • (2010) Helicobacter , vol.15 , pp. 154-159
    • Minakari, M.1    Jazi, A.H.D.2    Shavakhi, A.3    Moghareabed, N.4    Fatahi, F.5
  • 7
    • 44949243126 scopus 로고    scopus 로고
    • New concepts of resistance in the treatment of Helicobacter pylori infections
    • Graham D.Y., Shiotani A. New concepts of resistance in the treatment of Helicobacter pylori infections. Nat. Clin. Pract. Gastroenterol. Hepatol. 2008, 5:321-331.
    • (2008) Nat. Clin. Pract. Gastroenterol. Hepatol. , vol.5 , pp. 321-331
    • Graham, D.Y.1    Shiotani, A.2
  • 9
    • 0035234935 scopus 로고    scopus 로고
    • The biosynthesis of coenzyme A in bacteria
    • Begley T.P., Kinsland C., Strauss E. The biosynthesis of coenzyme A in bacteria. Vitam. Horm. 2001, 61:157-171.
    • (2001) Vitam. Horm. , vol.61 , pp. 157-171
    • Begley, T.P.1    Kinsland, C.2    Strauss, E.3
  • 10
    • 0021186069 scopus 로고
    • Metabolism of 4'-phosphopantetheine in Escherichia coli
    • Jackowski S., Rock C.O. Metabolism of 4'-phosphopantetheine in Escherichia coli. J. Bacteriol. 1984, 158:115-120.
    • (1984) J. Bacteriol. , vol.158 , pp. 115-120
    • Jackowski, S.1    Rock, C.O.2
  • 11
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti C.M., Boyd D.H., Rubin E.J. Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 2003, 48:77-84.
    • (2003) Mol. Microbiol. , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 12
    • 79955664160 scopus 로고    scopus 로고
    • Production and use of antimicrobial agents, European Patent Office WO0017387
    • W.V. Shaw, A. Lewendon, Production and use of antimicrobial agents, European Patent Office WO0017387, 2000.
    • (2000)
    • Shaw, W.V.1    Lewendon, A.2
  • 13
    • 0029084226 scopus 로고
    • The cytidylyltransferase superfamily- identification of the nucleotide-binding site and fold prediction
    • Bork P., Holm L., Koonin E.V., Sander C. The cytidylyltransferase superfamily- identification of the nucleotide-binding site and fold prediction. Proteins 1995, 22:259-266.
    • (1995) Proteins , vol.22 , pp. 259-266
    • Bork, P.1    Holm, L.2    Koonin, E.V.3    Sander, C.4
  • 14
    • 0033578920 scopus 로고    scopus 로고
    • Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli
    • Geerlof A., Lewendon A., Shaw W.V. Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli. J. Biol. Chem. 1999, 274:27105-27111.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27105-27111
    • Geerlof, A.1    Lewendon, A.2    Shaw, W.V.3
  • 15
    • 0033561042 scopus 로고    scopus 로고
    • The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity
    • Izard T., Geerlof A. The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity. EMBO J. 1999, 18:2021-2030.
    • (1999) EMBO J. , vol.18 , pp. 2021-2030
    • Izard, T.1    Geerlof, A.2
  • 16
    • 0036301087 scopus 로고    scopus 로고
    • The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism
    • Izard T. The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism. J. Mol. Biol. 2002, 315:487-495.
    • (2002) J. Mol. Biol. , vol.315 , pp. 487-495
    • Izard, T.1
  • 17
    • 4344604153 scopus 로고    scopus 로고
    • Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase
    • Morris V.K., Izard T. Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase. Protein Sci. 2004, 13:2547-2552.
    • (2004) Protein Sci. , vol.13 , pp. 2547-2552
    • Morris, V.K.1    Izard, T.2
  • 19
    • 0037478788 scopus 로고    scopus 로고
    • A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A
    • Izard T. A novel adenylate binding site confers phosphopantetheine adenylyltransferase interactions with coenzyme A. J. Bacteriol. 2003, 185:4074-4080.
    • (2003) J. Bacteriol. , vol.185 , pp. 4074-4080
    • Izard, T.1
  • 20
    • 0037352458 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori
    • Eom S.J., Ahn H.J., Kim H.W., Baek S.H., Suh S.W. Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori. Acta Crystal. D 2003, 59:561-562.
    • (2003) Acta Crystal. D , vol.59 , pp. 561-562
    • Eom, S.J.1    Ahn, H.J.2    Kim, H.W.3    Baek, S.H.4    Suh, S.W.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: a tutorial review
    • Lebowitz J., Lewis M.S., Schuck P. Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci. 2002, 11:2067-2079.
    • (2002) Protein Sci. , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 23
    • 38549150372 scopus 로고    scopus 로고
    • Mutagenesis study of rice nonspecific lipid transfer protein 2 reveals residues that contribute to structure and ligand binding
    • Cheng C.S., Chen M.N., Lai Y.T., Chen T., Lin K.F., Liu Y.J., Lyu P.C. Mutagenesis study of rice nonspecific lipid transfer protein 2 reveals residues that contribute to structure and ligand binding. Proteins 2008, 70:695-706.
    • (2008) Proteins , vol.70 , pp. 695-706
    • Cheng, C.S.1    Chen, M.N.2    Lai, Y.T.3    Chen, T.4    Lin, K.F.5    Liu, Y.J.6    Lyu, P.C.7
  • 24
    • 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. Macromol. Cryst. A 1997, 276:307-326.
    • (1997) Methods Enzymol. Macromol. Cryst. A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 1997, 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 26
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystal. D 1997, 53:240-255.
    • (1997) Acta Crystal. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 27
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystal. D 2004, 60:2126-2132.
    • (2004) Acta Crystal. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 28
  • 30
    • 11844271472 scopus 로고    scopus 로고
    • Overexpression and purification of Pyrococcus abyssi phosphopantetheine adenylyltransferase from an optimized synthetic gene for NMR studies
    • Nalezkova M., de Groot A., Graf M., Gans P., Blanchard L. Overexpression and purification of Pyrococcus abyssi phosphopantetheine adenylyltransferase from an optimized synthetic gene for NMR studies. Protein Expr. Purif. 2005, 39:296-306.
    • (2005) Protein Expr. Purif. , vol.39 , pp. 296-306
    • Nalezkova, M.1    de Groot, A.2    Graf, M.3    Gans, P.4    Blanchard, L.5
  • 31
    • 0037316987 scopus 로고    scopus 로고
    • Flexibility analysis of enzyme active sites by crystallographic temperature factors
    • Yuan Z., Zhao J., Wang Z.X. Flexibility analysis of enzyme active sites by crystallographic temperature factors. Protein Eng. 2003, 16:109-114.
    • (2003) Protein Eng. , vol.16 , pp. 109-114
    • Yuan, Z.1    Zhao, J.2    Wang, Z.X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.