2v6e: Difference between revisions

Revision as of 04:28, 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:2v6e.png

Template:STRUCTURE 2v6e

PROTELOMERASE TELK COMPLEXED WITH SUBSTRATE DNAPROTELOMERASE TELK COMPLEXED WITH SUBSTRATE DNA

Template:ABSTRACT PUBMED 17889664

About this StructureAbout this Structure

2V6E is a Single protein structure of sequence from Klebsiella phage phiko2. Full crystallographic information is available from OCA.

ReferenceReference

An interlocked dimer of the protelomerase TelK distorts DNA structure for the formation of hairpin telomeres., Aihara H, Huang WM, Ellenberger T, Mol Cell. 2007 Sep 21;27(6):901-13. PMID:17889664

Page seeded by OCA on Mon Jul 28 04:28:03 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2v6e.gif|left|200px]]
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 {{STRUCTURE_2v6e|  PDB=2v6e  |  SCENE=  }}
-'''PROTELOMERASE TELK COMPLEXED WITH SUBSTRATE DNA'''
+===PROTELOMERASE TELK COMPLEXED WITH SUBSTRATE DNA===
-==Overview==
+<!--
-The termini of linear chromosomes are protected by specialized DNA structures known as telomeres that also facilitate the complete replication of DNA ends. The simplest type of telomere is a covalently closed DNA hairpin structure found in linear chromosomes of prokaryotes and viruses. Bidirectional replication of a chromosome with hairpin telomeres produces a catenated circular dimer that is subsequently resolved into unit-length chromosomes by a dedicated DNA cleavage-rejoining enzyme known as a hairpin telomere resolvase (protelomerase). Here we report a crystal structure of the protelomerase TelK from Klebsiella oxytoca phage varphiKO2, in complex with the palindromic target DNA. The structure shows the TelK dimer destabilizes base pairing interactions to promote the refolding of cleaved DNA ends into two hairpin ends. We propose that the hairpinning reaction is made effectively irreversible by a unique protein-induced distortion of the DNA substrate that prevents religation of the cleaved DNA substrate.
+The line below this paragraph, {{ABSTRACT_PUBMED_17889664}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17889664 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17889664}}
 ==About this Structure==
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 [[Category: Protelomerase]]
 [[Category: Resolvase]]
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