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Volumn 321, Issue 5893, 2008, Pages 1179-1183

The structure of an open form of an E. coli mechanosensitive channel at 3.45 å resolution

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM; CYTOLOGY; MECHANORECEPTION; MEMBRANE;

EID: 50649125767     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1159262     Document Type: Article
Times cited : (176)

References (43)
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    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
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    • Pressure ratios were measured using the patch clamp technique, and experimental details are reported in the supporting online material (SOM) and in fig. S1.
    • Pressure ratios were measured using the patch clamp technique, and experimental details are reported in the supporting online material (SOM) and in fig. S1.
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    • Extensive details of the crystallography are given in the SOM and in fig. S5.
    • Extensive details of the crystallography are given in the SOM and in fig. S5.
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    • Clockwise is defined when looking along the sevenfold axis from the periplasm into the cytoplasm.
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    • The value for the free energy change reported for the mutants is calculated by proportionation, assuming a linear relation between the free energies of the closed-to-open transitions of MscS and of MscL. Our interpretation does not depend on this linearity
    • The value for the free energy change reported for the mutants is calculated by proportionation, assuming a linear relation between the free energies of the closed-to-open transitions of MscS and of MscL. Our interpretation does not depend on this linearity.
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    • Our research was supported by the Wellcome Trust (grants GR077564MA and 040174, Medical Research Council (G0400277, Unilever (UK, and Biotechnology Biological Sciences Research Council (BBSRC, BB/F003455/1, Structural biology used the facilities of the Scottish Structural Proteomics Facility funded by the Scottish Funding Council and BBSRC. We thank K. Johnson, T. Rasmussen, and F. Flett for their contributions to this work; D. Rees and R. Bass for advice on crystallization and for pre-release of x-ray intensities; and A. Leslie for a critical reading of the manuscript. Coordinates and data have been deposited in the Protein Data Bank () with accession number 2vv5
    • Our research was supported by the Wellcome Trust (grants GR077564MA and 040174), Medical Research Council (G0400277), Unilever (UK), and Biotechnology Biological Sciences Research Council (BBSRC) (BB/F003455/1). Structural biology used the facilities of the Scottish Structural Proteomics Facility funded by the Scottish Funding Council and BBSRC. We thank K. Johnson, T. Rasmussen, and F. Flett for their contributions to this work; D. Rees and R. Bass for advice on crystallization and for pre-release of x-ray intensities; and A. Leslie for a critical reading of the manuscript. Coordinates and data have been deposited in the Protein Data Bank (www.rcsb.org) with accession number 2vv5.


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