2ho0: Difference between revisions
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[[Image:2ho0.gif|left|200px]] | [[Image:2ho0.gif|left|200px]] | ||
'''Structure of a Hyper-cleavable Monomeric Fragment of Phage Lambda Repressor Containing the Cleavage Site Region''' | {{Structure | ||
|PDB= 2ho0 |SIZE=350|CAPTION= <scene name='initialview01'>2ho0</scene>, resolution 2.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Structure of a Hyper-cleavable Monomeric Fragment of Phage Lambda Repressor Containing the Cleavage Site Region''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HO0 is a [ | 2HO0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HO0 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16934834 16934834] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: virus/viral protein]] | [[Category: virus/viral protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:19:20 2008'' | ||
Revision as of 15:19, 20 March 2008
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| 2ho0, resolution 2.50Å | |||||||||||||
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| Ligands: | CA | ||||||||||||
| 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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