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Volumn 176, Issue 3, 2011, Pages 419-424

AcrB contamination in 2-D crystallization of membrane proteins: Lessons from a sodium channel and a putative monovalent cation/proton antiporter

Author keywords

2 D Crystal; 2dx; Continuous flow dialysis; Electron crystallography; Membrane proteins; Sparse matrix; Structural genomics

Indexed keywords

ANTIPORTER; GLYCOPROTEIN P; MULTIDRUG TRANSPORTER ACRB; PROTEIN MPSIL0171; PROTEIN NACHBAC; UNCLASSIFIED DRUG; VOLTAGE GATED SODIUM CHANNEL;

EID: 80455160120     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.09.005     Document Type: Article
Times cited : (17)

References (12)
  • 1
    • 12144271044 scopus 로고    scopus 로고
    • Evolutionary origins of eukaryotic sodium/proton exchangers
    • Brett C.L., Donowitz M., Rao R. Evolutionary origins of eukaryotic sodium/proton exchangers. Am. J. Physiol. 2005, 288:C223-C239.
    • (2005) Am. J. Physiol. , vol.288
    • Brett, C.L.1    Donowitz, M.2    Rao, R.3
  • 3
    • 0028926676 scopus 로고
    • Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli
    • Ma D., Cook D.N., Alberti M., Pon N.G., Nikaido H., et al. Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli. Mol. Microbiol. 1995, 16:45-55.
    • (1995) Mol. Microbiol. , vol.16 , pp. 45-55
    • Ma, D.1    Cook, D.N.2    Alberti, M.3    Pon, N.G.4    Nikaido, H.5
  • 4
    • 79955549892 scopus 로고    scopus 로고
    • Simplified bacterial "pore" provides insight into the assembly, stability and structure of sodium channels
    • McCusker E.C., D'Avanzo N., Nichols C.G., Wallace B.A. Simplified bacterial "pore" provides insight into the assembly, stability and structure of sodium channels. J. Biol. Chem. 2011, 286:16386-16391.
    • (2011) J. Biol. Chem. , vol.286 , pp. 16386-16391
    • McCusker, E.C.1    D'Avanzo, N.2    Nichols, C.G.3    Wallace, B.A.4
  • 5
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S., Nakashima R., Yamashita E., Yamaguchi A. Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 2002, 419:107-111.
    • (2002) Nature , vol.419 , pp. 107-111
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 6
    • 33748670458 scopus 로고    scopus 로고
    • Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    • Murakami S., Nakashima R., Yamashita E., Matsumoto T., Yamaguchi A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 2006, 443:173-179.
    • (2006) Nature , vol.443 , pp. 173-179
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Matsumoto, T.4    Yamaguchi, A.5
  • 7
    • 48649087167 scopus 로고    scopus 로고
    • Tetrameric bacterial sodium channels: characterization of structure, stability, and drug binding
    • Nurani G., Radford M., Charalambous K., O'Reilly A.O., Cronin N., et al. Tetrameric bacterial sodium channels: characterization of structure, stability, and drug binding. Biochemistry 2008, 47:8114-8121.
    • (2008) Biochemistry , vol.47 , pp. 8114-8121
    • Nurani, G.1    Radford, M.2    Charalambous, K.3    O'Reilly, A.O.4    Cronin, N.5
  • 8
    • 77956294944 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy-defined structure of the c-terminal domain of NaChBac and its role in channel assembly
    • Powl A.M., O'Reilly A.O., Miles A.J., Wallace B.A. Synchrotron radiation circular dichroism spectroscopy-defined structure of the c-terminal domain of NaChBac and its role in channel assembly. Proc. Natl. Acad. Sci. USA 2010, 107:14064-14069.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 14064-14069
    • Powl, A.M.1    O'Reilly, A.O.2    Miles, A.J.3    Wallace, B.A.4
  • 9
    • 60649117715 scopus 로고    scopus 로고
    • AcrB et al.: obstinate contaminants in a picogram scale. one more bottleneck in the membrane protein structure pipeline
    • Psakis G., Polaczek J., Essen L.O. AcrB et al.: obstinate contaminants in a picogram scale. one more bottleneck in the membrane protein structure pipeline. J. Struct. Biol. 2009, 166:107-111.
    • (2009) J. Struct. Biol. , vol.166 , pp. 107-111
    • Psakis, G.1    Polaczek, J.2    Essen, L.O.3
  • 10
    • 0035861457 scopus 로고    scopus 로고
    • A prokaryotic voltage-gated sodium channel
    • Ren D., Navarro B., Xu H., Yue L., Shi Q., et al. A prokaryotic voltage-gated sodium channel. Science 2001, 294:2372-2375.
    • (2001) Science , vol.294 , pp. 2372-2375
    • Ren, D.1    Navarro, B.2    Xu, H.3    Yue, L.4    Shi, Q.5
  • 11
    • 33748310520 scopus 로고    scopus 로고
    • Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
    • Seeger M.A., Schiefner A., Eicher T., Verrey F., Diederichs K., et al. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 2006, 313:1295-1298.
    • (2006) Science , vol.313 , pp. 1295-1298
    • Seeger, M.A.1    Schiefner, A.2    Eicher, T.3    Verrey, F.4    Diederichs, K.5
  • 12
    • 53749093441 scopus 로고    scopus 로고
    • There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization
    • Veesler D., Blangy S., Cambillau C., Sciara G. There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization. Acta Cryst. Sect. F Struct. Biol. Cryst. Commun. 2008, 64:880-885.
    • (2008) Acta Cryst. Sect. F Struct. Biol. Cryst. Commun. , vol.64 , pp. 880-885
    • Veesler, D.1    Blangy, S.2    Cambillau, C.3    Sciara, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.