title: Crystal structure of an activated response regulator bound to its target.
abstract: The chemotactic regulator CheY controls the direction of flagellar rotation in Escherichia coli. We have determined the crystal structure of BeF3--activated CheY from E. coli in complex with an N-terminal peptide derived from its target, FliM. The structure reveals that the first seven residues of the peptide pack against the beta4-H4 loop and helix H4 of CheY in an extended conformation, whereas residues 8-15 form two turns of helix and pack against the H4-beta5-H5 face. The peptide binds the only region of CheY that undergoes noticeable conformational change upon activation and would most likely be sandwiched between activated CheY and the remainder of FliM to reverse the direction of flagellar rotation.
authors.affiliation: Graduate Group in Biophysics, University of California, Berkeley, California 94720, USA.
authors.forename: S Y
authors.initials: SY
authors.lastname: Lee
authors.forename: H S
authors.initials: HS
authors.lastname: Cho
authors.forename: J G
authors.initials: JG
authors.lastname: Pelton
authors.forename: D
authors.initials: D
authors.lastname: Yan
authors.forename: R K
authors.initials: RK
authors.lastname: Henderson
authors.forename: D S
authors.initials: DS
authors.lastname: King
authors.forename: L
authors.initials: L
authors.lastname: Huang
authors.forename: S
authors.initials: S
authors.lastname: Kustu
authors.forename: E A
authors.initials: EA
authors.lastname: Berry
authors.forename: D E
authors.initials: DE
authors.lastname: Wemmer
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001608:Beryllium / Q000494:pharmacology; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004789:Enzyme Activation / Q000187:drug effects; D004926:Escherichia coli / Q000737:chemistry* / Q000201:enzymology / Q000502:physiology; D029968:Escherichia coli Proteins; D005407:Flagella / Q000502:physiology; D005459:Fluorides / Q000494:pharmacology; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D012399:Rotation; D016415:Sequence Alignment; D055672:Static Electricity
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D010446:Peptide Fragments; C000607606:cheY protein, E coli; C066821:FliM protein, Bacteria; C035982:beryllium fluoride; D001608:Beryllium; D005459:Fluorides