2ho0

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[[Image:2ho0.gif|left|200px]]
[[Image:2ho0.gif|left|200px]]
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{{Structure
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{{STRUCTURE_2ho0| PDB=2ho0 | SCENE= }}
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|RELATEDENTRY=[[1f39|1F39]], [[1jhc|1JHC]], [[1jhe|1JHE]], [[2hnf|2HNF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ho0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ho0 OCA], [http://www.ebi.ac.uk/pdbsum/2ho0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ho0 RCSB]</span>
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'''Structure of a Hyper-cleavable Monomeric Fragment of Phage Lambda Repressor Containing the Cleavage Site Region'''
'''Structure of a Hyper-cleavable Monomeric Fragment of Phage Lambda Repressor Containing the Cleavage Site Region'''
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[[Category: Bell, C E.]]
[[Category: Bell, C E.]]
[[Category: Ndjonka, D.]]
[[Category: Ndjonka, D.]]
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[[Category: virus/viral protein]]
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[[Category: Virus/viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:30:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:32:53 2008''
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Revision as of 03:30, 4 May 2008

Template:STRUCTURE 2ho0

Structure of a Hyper-cleavable Monomeric Fragment of Phage Lambda Repressor Containing the Cleavage Site Region


Overview

The key event in the switch from lysogenic to lytic growth of phage lambda is the self-cleavage of lambda repressor, which is induced by the formation of a RecA-ssDNA-ATP filament at a site of DNA damage. Lambda repressor cleaves itself at the peptide bond between Ala111 and Gly112, but only when bound as a monomer to the RecA-ssDNA-ATP filament. Here we have designed a hyper-cleavable fragment of lambda repressor containing the hinge and C-terminal domain (residues 101-229), in which the monomer-monomer interface is disrupted by two point mutations and a deletion of seven residues at the C terminus. This fragment crystallizes as a monomer and its structure has been determined to 1.8 A resolution. The hinge region, which bears the cleavage site, is folded over the active site of the C-terminal oligomerization domain (CTD) but with the cleavage site flipped out and exposed to solvent. Thus, the structure represents a non-cleavable conformation of the repressor, but one that is poised for cleavage after modest rearrangements that are presumably stabilized by binding to RecA. The structure provides a unique snapshot of lambda repressor in a conformation that sheds light on how its self-cleavage is tempered in the absence of RecA, as well as a framework for interpreting previous genetic and biochemical data concerning the RecA-mediated cleavage reaction.

About this Structure

2HO0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of a hyper-cleavable monomeric fragment of phage lambda repressor containing the cleavage site region., Ndjonka D, Bell CE, J Mol Biol. 2006 Sep 22;362(3):479-89. Epub 2006 Jul 15. PMID:16934834 Page seeded by OCA on Sun May 4 06:30:14 2008

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