Structural basis for ligand-regulated oligomerization of AraC

Science

Volumn 276, Issue 5311, 1997, Pages 421-425

  Soisson, Stephen M ^a   MacDougall Shackleton, Beth ^b   Schleif, Robert ^b   Wolberger, Cynthia ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b JOHNS HOPKINS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARABINOSE; REGULATOR PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ESCHERICHIA COLI; LIGAND BINDING; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

ARABINOSE; ARAC TRANSCRIPTION FACTOR; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DNA; HYDROGEN BONDING; LIGANDS; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; REPRESSOR PROTEINS; TRANSCRIPTION FACTORS;

ESCHERICHIA COLI;

EID: 0030964038     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.276.5311.421     Document Type: Article

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37. We thank A. Batchelor, E. Reisinger, J. Aishima, and M. Greisman for help with data collection; C. Ogata and R. Abramowitz of beamline X4A at the National Synchrotron Light Source for advice and technical support; and J. Berg, M. Amzel, and E. Lattman for comments on the manuscript. C. Becker, M. Nagypal, S. Jenkins, A. Favreau, M. Williams, and J. Withey helped with purification and crystallization efforts. We thank C. Turgeon and J. Hansen of the University of Texas Health Sciences Center at San Antonio for analyzing samples by analytical ultracentrifugation and A. Brünger and L. Rice for a prerelease version of X-PLOR for torsion angle dynamics refinement. Supported by the Howard Hughes Medical Institute (C.W. and beamlineX4A), the David and Lucile Packard Foundation (C.W.), and grant GM18277 from the National Institutes of Health (R.S.). Atomic coordinates have been deposited at the Brookhaven Protein Data Bank (accession numbers 2ARC and 2ARA).