1f4v
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(New page: 200px<br /><applet load="1f4v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f4v, resolution 2.22Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 12:30, 20 November 2007
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CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM
Overview
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.
About this Structure
1F4V is a Protein complex structure of sequences from Escherichia coli with MG, BEF and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of an activated response regulator bound to its target., Lee SY, Cho HS, Pelton JG, Yan D, Henderson RK, King DS, Huang L, Kustu S, Berry EA, Wemmer DE, Nat Struct Biol. 2001 Jan;8(1):52-6. PMID:11135671
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