1f4v

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[[Image:1f4v.jpg|left|200px]]
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{{Seed}}
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[[Image:1f4v.png|left|200px]]
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{{STRUCTURE_1f4v| PDB=1f4v | SCENE= }}
{{STRUCTURE_1f4v| PDB=1f4v | SCENE= }}
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'''CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM'''
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===CRYSTAL STRUCTURE OF ACTIVATED CHEY BOUND TO THE N-TERMINUS OF FLIM===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11135671}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11135671 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11135671}}
==About this Structure==
==About this Structure==
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[[Category: Peptide-protein complex]]
[[Category: Peptide-protein complex]]
[[Category: Response regulator]]
[[Category: Response regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:41:53 2008''

Revision as of 23:41, 30 June 2008

Template:STRUCTURE 1f4v

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

Template:ABSTRACT PUBMED 11135671

About this Structure

1F4V is a Protein complex structure of sequences from Escherichia coli. 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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