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2ho0

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|PDB= 2ho0 |SIZE=350|CAPTION= <scene name='initialview01'>2ho0</scene>, resolution 2.50&Aring;
|PDB= 2ho0 |SIZE=350|CAPTION= <scene name='initialview01'>2ho0</scene>, resolution 2.50&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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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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}}
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[[Category: Bell, C E.]]
[[Category: Bell, C E.]]
[[Category: Ndjonka, D.]]
[[Category: Ndjonka, D.]]
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[[Category: CA]]
 
[[Category: virus/viral protein]]
[[Category: virus/viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:19:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:32:53 2008''

Revision as of 00:32, 31 March 2008


PDB ID 2ho0

Drag the structure with the mouse to rotate
, resolution 2.50Å
Ligands:
Related: 1F39, 1JHC, 1JHE, 2HNF


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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