Structural basis of chaperone function and pilus biogenesis

Science

Volumn 285, Issue 5430, 1999, Pages 1058-1061

  Sauer, Frederic G ^a   Fütterer, Klaus ^a   Pinkner, Jerome S ^a   Dodson, Karen W ^a   Hultgren, Scott J ^a   Waksman, Gabriel ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE;

ARTICLE; BACTERIUM PILUS; CRYSTAL STRUCTURE; GRAM NEGATIVE BACTERIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; PROTEIN TRANSPORT;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FIMBRIAE PROTEINS; FIMBRIAE, BACTERIAL; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PERIPLASMIC PROTEINS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS); NEGIBACTERIA;

EID: 0039843096     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.285.5430.1058     Document Type: Article

References (39)

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22. 1, with cell dimensions a = 62.1 A, b = 63.6 A, and c = 92.7 A, and with one complex in the asymmetric unit. Native and SeMet data sets to 2.7 A and 2.5 A resolution, respectively, were collected on single flash-cooled crystals in the laboratory setting (native and SeMet-single data sets, Table 1). A SeMet PapD-PapK crystal was also used to collect multi-wavelength anomalous dispersion (MAD) data at four wavelengths to a resolution of 2.4 A at the National Synchrotron Light Source (NSLS) (SeMet-1 through -4, Table 1). All data were reduced and processed using the programs DENZO and SCALEPACK [ Z. Otwinoski, in Proceedings of the CCP4 Study Weekend, L. Sawyers, N. Isaacs, S. Bailey, Eds. (SERC Daresbury Laboratory, Warrington, UK, 1993), pp. 56-62].
23. 1, with cell dimensions a = 62.1 A, b = 63.6 A, and c = 92.7 A, and with one complex in the asymmetric unit. Native and SeMet data sets to 2.7 A and 2.5 A resolution, respectively, were collected on single flash-cooled crystals in the laboratory setting (native and SeMet-single data sets, Table 1). A SeMet PapD-PapK crystal was also used to collect multi-wavelength anomalous dispersion (MAD) data at four wavelengths to a resolution of 2.4 A at the National Synchrotron Light Source (NSLS) (SeMet-1 through -4, Table 1). All data were reduced and processed using the programs DENZO and SCALEPACK [ Z. Otwinoski, in Proceedings of the CCP4 Study Weekend, L. Sawyers, N. Isaacs, S. Bailey, Eds. (SERC Daresbury Laboratory, Warrington, UK, 1993), pp. 56-62].
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26. 2-terminus. All residues in PapK and PapD are located in either the most favored or the allowed regions of the Ramachandran plot [ G. N. Ramachandran and V. Sasisekharan, Adv. Protein Chem. 23, 283 (1968)].
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28. 2-terminus. All residues in PapK and PapD are located in either the most favored or the allowed regions of the Ramachandran plot [ G. N. Ramachandran and V. Sasisekharan, Adv. Protein Chem. 23, 283 (1968)].
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39. We thank A. B. Herr for help with MAD data collection, G. Soto and D. Hung far help in preparing figures, and C. Ogata and the staff of beamline X4A at NSLS. Supported by NIH grants RO1DK51406 and RO1AI29549 (S.J.H.) and RO1GM54033 (G.W.).