메뉴 건너뛰기




Volumn 493, Issue 7431, 2013, Pages 255-258

Structure of the proton-gated urea channel from the gastric pathogen Helicobacter pylori

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; PHENYLALANINE; THIOUREA; TRYPTOPHAN; UREA;

EID: 84872146541     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11684     Document Type: Article
Times cited : (75)

References (33)
  • 1
    • 0029076049 scopus 로고
    • The prevalence of Helicobacter pylori infection in different countries
    • Pounder, R. E. & Ng, D. The prevalence of Helicobacter pylori infection in different countries. Aliment. Pharmacol. Ther. 9, 33-39 (1995).
    • (1995) Aliment. Pharmacol. Ther , vol.9 , pp. 33-39
    • Pounder, R.E.1    Ng, D.2
  • 2
    • 0036370334 scopus 로고    scopus 로고
    • Helicobacter pylori and gastrointestinal tract adenocarcinomas
    • Peek, R. M. & Blaser, M. J. Helicobacter pylori and gastrointestinal tract adenocarcinomas. Nature Rev. Cancer 2, 28-37 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 28-37
    • Peek, R.M.1    Blaser, M.J.2
  • 3
    • 0031661885 scopus 로고    scopus 로고
    • The Helicobacter pylori UreI protein is not involved in urease activity but is essential for bacterial survival in vivo
    • Skouloubris, S., Thiberge, J. M., Labigne, A. & De Reuse, H. The Helicobacter pylori UreI protein is not involved in urease activity but is essential for bacterial survival in vivo. Infect. Immun. 66, 4517-4521 (1998).
    • (1998) Infect. Immun , vol.66 , pp. 4517-4521
    • Skouloubris, S.1    Thiberge, J.M.2    Labigne, A.3    De Reuse, H.4
  • 4
    • 0034695684 scopus 로고    scopus 로고
    • H1-gated urea channel: The link between Helicobacter pylori urease and gastric colonization
    • Weeks, D. L., Eskandari, S., Scott, D. R. & Sachs, G. A. H1-gated urea channel: the link between Helicobacter pylori urease and gastric colonization. Science 287, 482-485 (2000).
    • (2000) Science , vol.287 , pp. 482-485
    • Weeks, D.L.1    Eskandari, S.2    Scott, D.R.3    Sachs, G.A.4
  • 5
    • 77954704743 scopus 로고    scopus 로고
    • Helicobacter pylori treatment in the era of increasing antibiotic resistance
    • Graham, D. Y. & Fischbach, L. Helicobacter pylori treatment in the era of increasing antibiotic resistance. Gut 59, 1143-1153 (2010).
    • (2010) Gut , vol.59 , pp. 1143-1153
    • Graham, D.Y.1    Fischbach, L.2
  • 6
    • 0036303568 scopus 로고    scopus 로고
    • Mechanisms of acid resistance due to the urease system of Helicobacter pylori
    • Scott, D. R., Marcus, E. A., Weeks, D. L. & Sachs, G. Mechanisms of acid resistance due to the urease system of Helicobacter pylori. Gastroenterology 123, 187-195 (2002).
    • (2002) Gastroenterology , vol.123 , pp. 187-195
    • Scott, D.R.1    Marcus, E.A.2    Weeks, D.L.3    Sachs, G.4
  • 7
    • 79954784829 scopus 로고    scopus 로고
    • Molecular aspects of bacterial pHsensing and homeostasis
    • Krulwich, T. A., Sachs, G.&Padan, E. Molecular aspects of bacterial pHsensing and homeostasis. Nature Rev. Microbiol. 9, 330-343 (2011).
    • (2011) Nature Rev. Microbiol , vol.9 , pp. 330-343
    • Krulwich, T.A.1    Sachs, G.2    Padan, E.3
  • 8
    • 0029815909 scopus 로고    scopus 로고
    • The effect of environmental pH on the proton motive force of Helicobacter pylori
    • Meyer-Rosberg, K., Scott, D. R., Rex, D., Melchers, K. & Sachs, G. The effect of environmental pH on the proton motive force of Helicobacter pylori. Gastroenterology 111, 886-900 (1996).
    • (1996) Gastroenterology , vol.111 , pp. 886-900
    • Meyer-Rosberg, K.1    Scott, D.R.2    Rex, D.3    Melchers, K.4    Sachs, G.5
  • 9
    • 0033609904 scopus 로고    scopus 로고
    • Structure of bacteriorhodopsin at 1.55A resolution
    • Luecke, H. et al. Structure of bacteriorhodopsin at 1.55A resolution. J. Mol. Biol. 291, 899-911 (1999).
    • (1999) J. Mol. Biol , vol.291 , pp. 899-911
    • Luecke, H.1
  • 10
    • 80053584625 scopus 로고    scopus 로고
    • Transport kinetics and selectivity of HpUreI, the urea channel from Helicobacter pylori
    • Gray, L. R., Gu, S. X., Quick, M. & Khademi, S. Transport kinetics and selectivity of HpUreI, the urea channel from Helicobacter pylori. Biochemistry 50, 8656-8663 (2011).
    • (2011) Biochemistry , vol.50 , pp. 8656-8663
    • Gray, L.R.1    Gu, S.X.2    Quick, M.3    Khademi, S.4
  • 11
    • 84863197430 scopus 로고    scopus 로고
    • A urea channel from Bacillus cereus reveals a novel hexameric structure
    • Huysmans, G. H. et al. A urea channel from Bacillus cereus reveals a novel hexameric structure. Biochem. J. 445, 157-166 (2012).
    • (2012) Biochem. J , vol.445 , pp. 157-166
    • Huysmans, G.H.1
  • 12
    • 0242497235 scopus 로고    scopus 로고
    • Structure of mitochondrial ATP/ADP carrier in complex with carboxyatractyloside
    • Pebay-Peyroula, E. et al. Structure of mitochondrial ATP/ADP carrier in complex with carboxyatractyloside. Nature 426, 39-44 (2003).
    • (2003) Nature , vol.426 , pp. 39-44
    • Pebay-Peyroula, E.1
  • 13
    • 72049114961 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of the kidney urea transporter
    • Levin, E. J., Quick, M. & Zhou, M. Crystal structure of a bacterial homologue of the kidney urea transporter. Nature 462, 757-761 (2009).
    • (2009) Nature , vol.462 , pp. 757-761
    • Levin, E.J.1    Quick, M.2    Zhou, M.3
  • 14
    • 84863944898 scopus 로고    scopus 로고
    • Structure and permeation mechanism of a mammalian urea transporter
    • Levin, E. J. et al. Structure and permeation mechanism of a mammalian urea transporter. Proc. Natl Acad. Sci. USA 109, 11194-11199 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 11194-11199
    • Levin, E.J.1
  • 15
    • 0034932504 scopus 로고    scopus 로고
    • Sites of pH regulation of the urea channel of Helicobacter pylori
    • Weeks, D. L. & Sachs, G. Sites of pH regulation of the urea channel of Helicobacter pylori. Mol. Microbiol. 40, 1249-1259 (2001).
    • (2001) Mol. Microbiol , vol.40 , pp. 1249-1259
    • Weeks, D.L.1    Sachs, G.2
  • 16
    • 79954580862 scopus 로고    scopus 로고
    • PH-dependent gating in a FocA formate channel
    • Lua W. et al. pH-dependent gating in a FocA formate channel. Science 332, 352-354 (2011).
    • (2011) Science , vol.332 , pp. 352-354
    • Lua, W.1
  • 18
    • 73849124969 scopus 로고    scopus 로고
    • Cytoplasmic histidine kinase (HP0244-regulated assembly of urease with UreI, a channel for urea and its metabolites, CO2, NH3 and NH4, 1 is necessary for acid survival of Helicobacter pylori
    • Scott, D. R. et al. Cytoplasmic histidine kinase (HP0244)-regulated assembly of urease with UreI, a channel for urea and its metabolites, CO2, NH3 and NH4 1, is necessary for acid survival of Helicobacter pylori. J. Bacteriol. 192, 94-103 (2010).
    • (2010) J. Bacteriol. , vol.192 , pp. 94-103
    • Scott, D.R.1
  • 19
    • 0037339018 scopus 로고    scopus 로고
    • Medium pH-dependent redistribution of the urease of Helicobacter pylori
    • Hong, W. et al. Medium pH-dependent redistribution of the urease of Helicobacter pylori. J. Med. Microbiol. 52, 211-216 (2002).
    • (2002) J. Med. Microbiol , vol.52 , pp. 211-216
    • Hong, W.1
  • 20
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • Gonen, T., Sliz, P., Kistler, J., Chen, Y. & Walz, T. Aquaporin-0 membrane junctions reveal the structure of a closed water pore. Nature 429, 193-197 (2004).
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Chen, Y.4    Walz, T.5
  • 21
    • 77958551193 scopus 로고    scopus 로고
    • APBSmem: A graphical interface for electrostatic calculations at the membrane
    • Callenberg, K. M. et al. APBSmem: a graphical interface for electrostatic calculations at the membrane. PLoS ONE 5, e12722 (2010).
    • (2010) PLoS ONE , vol.5
    • Callenberg, K.M.1
  • 22
    • 77953002925 scopus 로고    scopus 로고
    • Detecting internally symmetric protein structures
    • Kim, C., Basner, J.&Lee, B. Detecting internally symmetric protein structures.BMC Bioinformatics 11, 303-318 (2010).
    • (2010) BMC Bioinformatics , vol.11 , pp. 303-318
    • Kim, C.1    Basner, J.2    Lee, B.3
  • 27
    • 0033198415 scopus 로고    scopus 로고
    • Error estimation and bias correction in phase-improvement calculations
    • Cowtan, K. Error estimation and bias correction in phase-improvement calculations. Acta Crystallogr. D Biol. Crystallogr. 55, 1555-1567 (1999).
    • (1999) Acta Crystallogr. D Biol. Crystallogr , vol.55 , pp. 1555-1567
    • Cowtan, K.1
  • 28
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 29
    • 33747002198 scopus 로고    scopus 로고
    • Knowledge-based real-space explorations for low-resolution structure determination
    • Furnham, N. et al. Knowledge-based real-space explorations for low-resolution structure determination. Structure 14, 1313-1320 (2006).
    • (2006) Structure , vol.14 , pp. 1313-1320
    • Furnham, N.1
  • 30
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong, M. et al. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA 103, 8060-8065 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8060-8065
    • Strong, M.1
  • 31
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn, M. D., Murshudov, G. N. & Papiz, M. Z. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374, 300-321 (2003).
    • (2003) Methods Enzymol , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 32
    • 0033958917 scopus 로고    scopus 로고
    • Expression of the Helicobacter pylori ureI gene is required for acidic pH activation of cytoplasmic urease
    • Scott, D. R. et al. Expression of the Helicobacter pylori ureI gene is required for acidic pH activation of cytoplasmic urease. Infect. Immun. 68, 470-477 (2000).
    • (2000) Infect. Immun , vol.68 , pp. 470-477
    • Scott, D.R.1
  • 33
    • 85012361915 scopus 로고
    • The nonelectrolyte permeability of planar lipid bilayer membranes
    • Orbach, E. & Finkelstein, A. The nonelectrolyte permeability of planar lipid bilayer membranes. J. Gen. Physiol. 75, 427-436 (1980).
    • (1980) J. Gen. Physiol , vol.75 , pp. 427-436
    • Orbach, E.1    Finkelstein, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.