1z1b: Difference between revisions

Revision as of 20:42, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1z1b.png

Template:STRUCTURE 1z1b

Crystal structure of a lambda integrase dimer bound to a COC' core siteCrystal structure of a lambda integrase dimer bound to a COC' core site

Template:ABSTRACT PUBMED 15973401

About this StructureAbout this Structure

1Z1B is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

ReferenceReference

A structural basis for allosteric control of DNA recombination by lambda integrase., Biswas T, Aihara H, Radman-Livaja M, Filman D, Landy A, Ellenberger T, Nature. 2005 Jun 23;435(7045):1059-66. PMID:15973401

Page seeded by OCA on Mon Jul 28 20:41:56 2008

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OCA

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-'''Crystal structure of a lambda integrase dimer bound to a COC' core site'''
+===Crystal structure of a lambda integrase dimer bound to a COC' core site===
-==Overview==
+<!--
-Site-specific DNA recombination is important for basic cellular functions including viral integration, control of gene expression, production of genetic diversity and segregation of newly replicated chromosomes, and is used by bacteriophage lambda to integrate or excise its genome into and out of the host chromosome. lambda recombination is carried out by the bacteriophage-encoded integrase protein (lambda-int) together with accessory DNA sites and associated bending proteins that allow regulation in response to cell physiology. Here we report the crystal structures of lambda-int in higher-order complexes with substrates and regulatory DNAs representing different intermediates along the reaction pathway. The structures show how the simultaneous binding of two separate domains of lambda-int to DNA facilitates synapsis and can specify the order of DNA strand cleavage and exchange. An intertwined layer of amino-terminal domains bound to accessory (arm) DNAs shapes the recombination complex in a way that suggests how arm binding shifts the reaction equilibrium in favour of recombinant products.
+The line below this paragraph, {{ABSTRACT_PUBMED_15973401}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15973401 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15973401}}
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 [[Category: Radman-Livaja, M.]]
 [[Category: Protein-dna complex]]
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