X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli

Science

Volumn 285, Issue 5430, 1999, Pages 1061-1066

  Choudhury, Devapriya ^a   Thompson, Andrew ^a   Stojanoff, Vivian ^a   Langermann, Solomon ^a   Pinkner, Jerome ^a   Hultgren, Scott J ^a   Knight, Stefan D ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; CHAPERONE;

ARTICLE; BACTERIUM PILUS; CARBOXY TERMINAL SEQUENCE; ESCHERICHIA COLI; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; RECEPTOR BINDING; STRUCTURE ANALYSIS;

ADHESINS, BACTERIAL; ADHESINS, ESCHERICHIA COLI; AMINO ACID SEQUENCE; BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIAL PROTEINS; CHLORPROPAMIDE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FIMBRIAE PROTEINS; FIMBRIAE, BACTERIAL; HYDROGEN BONDING; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS); ENTEROBACTERIACEAE; ESCHERICHIA COLI;

EID: 0033551911     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.285.5430.1061     Document Type: Article

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30. Crystallographic software: HKL2000 [Z. Otwinowski and W. Minor, Methods Enzymol. 276, 307 (1997)]; CCP4 processing package [CCP4, Acta Crystallogr. D50, 760 (1994)]; SOLVE [T. C. Terwilliger and J. Berendzen, ibid. D53, 571 (1997)]; RSPS [ S. D. Knight, I. Andersson, C.-I. Brändén, J. Mol. Biol. 215, 113 (1990)]; SHARP [E. de la Fortelle and G. Bricogne, Methods Enzymol. 276, 472 (1997)]; DM [K. D. Cowtan, Joint CCP4 ESF-EACBM Newsl. Protein Crystallogr. 31, 34 (1994)] ; O [T. A. Jones, J.-Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. A47, 110 (1991)]; X-PLOR [ A. T. Brünger, X-PLOR Manual (Version 3.1): A System for X-ray Crystallography and NMR (Yale Univ. Press, New Haven, CT, 1993)]; REFMAC [ G. N. Murshudov, A. A. Vagin, E. J. Dodson, Acta Crystallogr. D53, 240 (1997)].
31. Crystallographic software: HKL2000 [Z. Otwinowski and W. Minor, Methods Enzymol. 276, 307 (1997)]; CCP4 processing package [CCP4, Acta Crystallogr. D50, 760 (1994)]; SOLVE [T. C. Terwilliger and J. Berendzen, ibid. D53, 571 (1997)]; RSPS [ S. D. Knight, I. Andersson, C.-I. Brändén, J. Mol. Biol. 215, 113 (1990)]; SHARP [E. de la Fortelle and G. Bricogne, Methods Enzymol. 276, 472 (1997)]; DM [K. D. Cowtan, Joint CCP4 ESF-EACBM Newsl. Protein Crystallogr. 31, 34 (1994)] ; O [T. A. Jones, J.-Y. Zou, S. W. Cowan, M. Kjeldgaard, Acta Crystallogr. A47, 110 (1991)]; X-PLOR [ A. T. Brünger, X-PLOR Manual (Version 3.1): A System for X-ray Crystallography and NMR (Yale Univ. Press, New Haven, CT, 1993)]; REFMAC [ G. N. Murshudov, A. A. Vagin, E. J. Dodson, Acta Crystallogr. D53, 240 (1997)].
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34. 22 in the gene-derived sequence, which is the expected start of the mature FimH chain [ M. S. Hanson, J. Hempel, C. B. Brinton Jr., J. Bacteriol. 170, 3350 (1988)]. To distinguish residues in the adhesin from residues in the chaperone, FimH residues will be denoted by an H, and FimC residues by a C, after the residue number.
35. 22 in the gene-derived sequence, which is the expected start of the mature FimH chain [ M. S. Hanson, J. Hempel, C. B. Brinton Jr., J. Bacteriol. 170, 3350 (1988)]. To distinguish residues in the adhesin from residues in the chaperone, FimH residues will be denoted by an H, and FimC residues by a C, after the residue number.
36. Interface residues were defined as having a difference in solvent accessibility [S. Miller, J. Janin, A. M. Lesk, C. Chothia, J. Mol. Biol. 196, 641 (1987)] between the subunit in the complex and removed from the complex exceeding 10 percentage points.
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38. We thank A. Revel and J. Burlein for technical assistance and advice; the staff at the Max II synchrotron in Lund; H. Eklund, J. Hajdu, A. Jones, and S. Ramaswamy for discussions and reading of the manuscript; and J. Berglund for help with the figures. Supported by grants from the Swedish Research Council NFR and the Swedish Foundation for Strategic Research (Structural Biology Network) (S.D.K.), and by National Institutes of Health grants RO1DK51406 and RO1AI29549 (S.J.H.). The coordinates have been deposited at the Research Col-laboratory for Structural Bioinformatics Protein Data Bank (code 1QUN).