1F4V

CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM

Summary for 1F4V

• Entry DOI: 10.2210/pdb1f4v/pdb
• Related: 1DJM 1FQW 3CHY
• Descriptor: CHEMOTAXIS CHEY PROTEIN, FLAGELLAR MOTOR SWITCH PROTEIN, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: response regulator, peptide-protein complex, bacterial signal transduction, bef3, signaling protein
• Biological source: Escherichia coli; More
• Cellular location: Cell inner membrane; Peripheral membrane protein: P06974
• Total number of polymer chains: 6
• Total formula weight: 47468.18

Authors

Lee, S.Y.,Cho, H.S.,Pelton, J.G.,Yan, D.,Henderson, R.K.,King, D.,Huang, L.S.,Kustu, S.,Berry, E.A.,Wemmer, D.E. (deposition date: 2000-06-10, release date: 2001-01-17, Last modification date: 2024-02-07)

Primary citation

Lee, S.Y.,Cho, H.S.,Pelton, J.G.,Yan, D.,Henderson, R.K.,King, D.S.,Huang, L.,Kustu, S.,Berry, E.A.,Wemmer, D.E.
Crystal structure of an activated response regulator bound to its target.
Nat.Struct.Biol., 8:52-56, 2001

PubMed 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.

PubMed: 11135671
DOI: 10.1038/83053

Experimental method

X-RAY DIFFRACTION (2.22 Å)