메뉴 건너뛰기




Volumn 105, Issue 22, 2008, Pages 7696-7701

Insights into the stator assembly of the Vibrio flagellar motor from the crystal structure of MotY

Author keywords

Bacterial flagellum; Peptidoglycan binding; Sodium driven motor; T ring

Indexed keywords

BACTERIAL PROTEIN; BINDING PROTEIN; MOLECULAR MOTOR; PEPTIDOGLYCAN; PROTEIN MOTY; MOTY PROTEIN, VIBRIO; OUTER MEMBRANE PROTEIN;

EID: 45549087026     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0800308105     Document Type: Article
Times cited : (59)

References (31)
  • 1
    • 0041673353 scopus 로고    scopus 로고
    • The rotary motor of bacterial flagella
    • Berg HC (2003) The rotary motor of bacterial flagella. Annu Rev Biochem 72:19-54.
    • (2003) Annu Rev Biochem , vol.72 , pp. 19-54
    • Berg, H.C.1
  • 2
    • 1842588296 scopus 로고    scopus 로고
    • The bacterial flagellar motor: Structure and function of a complex molecular machine
    • Kojima S, Blair DF (2004) The bacterial flagellar motor: Structure and function of a complex molecular machine. Int Rev Cytol 233:93-134.
    • (2004) Int Rev Cytol , vol.233 , pp. 93-134
    • Kojima, S.1    Blair, D.F.2
  • 4
    • 0034719374 scopus 로고    scopus 로고
    • Torque-generating units of the flagellar motor of Escherichia coli have a high duty ratio
    • Ryu WS, Berry RM, Berg HC (2000) Torque-generating units of the flagellar motor of Escherichia coli have a high duty ratio. Nature 403:444-447.
    • (2000) Nature , vol.403 , pp. 444-447
    • Ryu, W.S.1    Berry, R.M.2    Berg, H.C.3
  • 5
    • 27144534030 scopus 로고    scopus 로고
    • Direct observation of steps in rotation of the bacterial flagellar motor
    • Sowa Y, et al. (2005) Direct observation of steps in rotation of the bacterial flagellar motor. Nature 437:916-919.
    • (2005) Nature , vol.437 , pp. 916-919
    • Sowa, Y.1
  • 6
    • 0030792908 scopus 로고    scopus 로고
    • Putative channel components for the fast-rotating sodium-driven flagellar motor of a maine bacterium
    • Asai Y, et al. (1997) Putative channel components for the fast-rotating sodium-driven flagellar motor of a maine bacterium. J Bacteriol 179:5104-5110.
    • (1997) J Bacteriol , vol.179 , pp. 5104-5110
    • Asai, Y.1
  • 7
    • 0029919952 scopus 로고    scopus 로고
    • Cloning and characterization of motY, a gene coding for a component of the sodium-driven flagellar motor in Vibrio alginolyticus
    • Okunishi I, Kawagishi I, Homma M (1996) Cloning and characterization of motY, a gene coding for a component of the sodium-driven flagellar motor in Vibrio alginolyticus. J Bacteriol 178:2409-2415.
    • (1996) J Bacteriol , vol.178 , pp. 2409-2415
    • Okunishi, I.1    Kawagishi, I.2    Homma, M.3
  • 8
    • 0035667275 scopus 로고    scopus 로고
    • Cloning and characterization of motX, a Vibrio alginolyticus sodium-driven flagellar motor gene
    • Okabe M, Yakushi T, Asai Y, Homma M (2001) Cloning and characterization of motX, a Vibrio alginolyticus sodium-driven flagellar motor gene. J Biochem (Tokyo) 130:879-884.
    • (2001) J Biochem (Tokyo) , vol.130 , pp. 879-884
    • Okabe, M.1    Yakushi, T.2    Asai, Y.3    Homma, M.4
  • 9
    • 0034051670 scopus 로고    scopus 로고
    • +-driven polar flagellar motor component of Vibrio alginolyticus
    • +-driven polar flagellar motor component of Vibrio alginolyticus. J Biol Chem 275:5718-5722.
    • (2000) J Biol Chem , vol.275 , pp. 5718-5722
    • Sato, K.1    Homma, M.2
  • 10
    • 0034733660 scopus 로고    scopus 로고
    • +-driven polar flagellar motor component of Vibrio alginolyticus
    • +-driven polar flagellar motor component of Vibrio alginolyticus. J Biol Chem 275:20223-20228.
    • (2000) J Biol Chem , vol.275 , pp. 20223-20228
    • Sato, K.1    Homma, M.2
  • 11
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch A, Schulz GE (1998) Structure of the outer membrane protein A transmembrane domain. Nat Struct Biol 5:1013-1017.
    • (1998) Nat Struct Biol , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 12
    • 1242342946 scopus 로고    scopus 로고
    • Deletion analysis of the peptidoglycan-associated lipoprotein Pal reveals three independent binding sequences including a TolA box
    • Cascales E, Lloubes R (2004) Deletion analysis of the peptidoglycan-associated lipoprotein Pal reveals three independent binding sequences including a TolA box. Mol Microbiol 51:873-885.
    • (2004) Mol Microbiol , vol.51 , pp. 873-885
    • Cascales, E.1    Lloubes, R.2
  • 13
    • 1442325407 scopus 로고    scopus 로고
    • Structure of the OmpA-like domain of RmpM from Neisseria meningitidis
    • Grizot S, Buchanan SK (2004) Structure of the OmpA-like domain of RmpM from Neisseria meningitidis. Mol Microbiol 51:1027-1037.
    • (2004) Mol Microbiol , vol.51 , pp. 1027-1037
    • Grizot, S.1    Buchanan, S.K.2
  • 14
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • De Mot R, Vanderleyden J (1994) The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol Microbiol 12:333-334.
    • (1994) Mol Microbiol , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 15
    • 0029092472 scopus 로고
    • Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins
    • Koebnik R (1995) Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol Microbiol 16:1269-1270.
    • (1995) Mol Microbiol , vol.16 , pp. 1269-1270
    • Koebnik, R.1
  • 16
    • 33745877129 scopus 로고    scopus 로고
    • Roles of the intramolecular disulfide bridge in MotX and MotY, the specific proteins for sodium-driven motors in Vibrio spp
    • Yagasaki J, Okabe M, Kurebayashi R, Yakushi T, Homma M (2006) Roles of the intramolecular disulfide bridge in MotX and MotY, the specific proteins for sodium-driven motors in Vibrio spp. J Bacteriol 188:5308-5314.
    • (2006) J Bacteriol , vol.188 , pp. 5308-5314
    • Yagasaki, J.1    Okabe, M.2    Kurebayashi, R.3    Yakushi, T.4    Homma, M.5
  • 17
    • 0036033221 scopus 로고    scopus 로고
    • MotX and MotY, specific components of the sodium-driven flagellar motor, colocalize to the outer membrane in Vibrio alginolyticus
    • Okabe M, Yakushi T, Kojima M, Homma M (2002) MotX and MotY, specific components of the sodium-driven flagellar motor, colocalize to the outer membrane in Vibrio alginolyticus. Mol Microbiol 46:125-134.
    • (2002) Mol Microbiol , vol.46 , pp. 125-134
    • Okabe, M.1    Yakushi, T.2    Kojima, M.3    Homma, M.4
  • 18
    • 21844451390 scopus 로고    scopus 로고
    • Interactions of MotX with MotY and with the PomA/PomB sodium ion channel complex of the Vibrio alginolyticus polar flagellum
    • Okabe M, Yakushi T, Homma M (2005) Interactions of MotX with MotY and with the PomA/PomB sodium ion channel complex of the Vibrio alginolyticus polar flagellum. J Biol Chem 280:25659-25664.
    • (2005) J Biol Chem , vol.280 , pp. 25659-25664
    • Okabe, M.1    Yakushi, T.2    Homma, M.3
  • 20
    • 33847126169 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of MotY, a stator component of the Vibrio alginolyticus polar flagellar motor
    • Shinohara A, et al. (2007) Crystallization and preliminary X-ray analysis of MotY, a stator component of the Vibrio alginolyticus polar flagellar motor. Acta Crystallogr F 63:89-92.
    • (2007) Acta Crystallogr F , vol.63 , pp. 89-92
    • Shinohara, A.1
  • 21
    • 33144490288 scopus 로고    scopus 로고
    • Peptidoglycan recognition by Pal, an outer membrane lipoprotein
    • Parsons LM, Lin F, Orban J (2006) Peptidoglycan recognition by Pal, an outer membrane lipoprotein. Biochemistry 45:2122-2128.
    • (2006) Biochemistry , vol.45 , pp. 2122-2128
    • Parsons, L.M.1    Lin, F.2    Orban, J.3
  • 22
    • 18744434661 scopus 로고    scopus 로고
    • +-driven motor of Escherichia coli
    • +-driven motor of Escherichia coli. J Bacteriol 182:4234-4240.
    • (2000) J Bacteriol , vol.182 , pp. 4234-4240
    • Gosink, K.K.1    Häse, C.C.2
  • 24
    • 4544233498 scopus 로고    scopus 로고
    • The complex flagellar torque generator of Pseudomonas aeruginosa
    • Doyle TB, Hawkins AC, McCarter LL (2004) The complex flagellar torque generator of Pseudomonas aeruginosa. J Bacteriol 186:6341-6350.
    • (2004) J Bacteriol , vol.186 , pp. 6341-6350
    • Doyle, T.B.1    Hawkins, A.C.2    McCarter, L.L.3
  • 25
  • 26
    • 0028103275 scopus 로고
    • Number 4, The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project, Number 4, The CCP4 suite: Programs for protein crystallography. (1994) Acta Crystallogr D 50:760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 27
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger TC, Berendzen J (1999) Automated structure solution for MIR and MAD. Acta Crystallogr D 55:849-861.
    • (1999) Acta Crystallogr D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW , Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D 54:905-921.
    • (1998) Acta Crystallogr D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 30
    • 0028040922 scopus 로고
    • Removal of the periplasmic DNase before electroporation enhances efficiency of transformation in a marine bacterium Vibrio alginolyticus
    • Kawagishi I, Okunishi I, Homma M, Imae Y (1994) Removal of the periplasmic DNase before electroporation enhances efficiency of transformation in a marine bacterium Vibrio alginolyticus. Microbiology 140:2355-2361.
    • (1994) Microbiology , vol.140 , pp. 2355-2361
    • Kawagishi, I.1    Okunishi, I.2    Homma, M.3    Imae, Y.4
  • 31
    • 32944458166 scopus 로고    scopus 로고
    • Regulation of polar flagellar number by the flhF and flhG genes in Vibrio alginolyticus
    • Kusumoto A, et al. (2006) Regulation of polar flagellar number by the flhF and flhG genes in Vibrio alginolyticus. J Biochem (Tokyo) 139:113-121.
    • (2006) J Biochem (Tokyo) , vol.139 , pp. 113-121
    • Kusumoto, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.