2v6e | pdb_00002v6e

protelomerase TelK complexed with substrate DNA

spinqualitylabelsall models 2v6e, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2v6e is a 6 chain structure with sequence from Escherichia virus N15 and Klebsiella phage phiKO2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: VO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6UAV6_9CAUD Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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