4E0Z

Protelomerase tela R205A covalently complexed with substrate DNA

Summary for 4E0Z

• Entry DOI: 10.2210/pdb4e0z/pdb
• Related: 4DWP 4E0G 4E0J 4E0P 4E0Y 4E10
• Descriptor: Protelomerase, DNA (5'-D(*CP*AP*TP*AP*AP*TP*AP*AP*CP*AP*AP*TP*A)-3'), DNA (5'-D(*TP*CP*A*TP*GP*AP*TP*AP*TP*TP*GP*TP*TP*AP*TP*TP*AP*TP*G)-3'), ... (6 entities in total)
• Functional Keywords: protelemorase, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Agrobacterium tumefaciens
• Total number of polymer chains: 3
• Total formula weight: 63044.08

Authors

Shi, K.,Aihara, H. (deposition date: 2012-03-05, release date: 2013-02-13, Last modification date: 2024-10-30)

Primary citation

Shi, K.,Huang, W.M.,Aihara, H.
An enzyme-catalyzed multistep DNA refolding mechanism in hairpin telomere formation.
Plos Biol., 11:e1001472-e1001472, 2013

PubMed Abstract: Hairpin telomeres of bacterial linear chromosomes are generated by a DNA cutting-rejoining enzyme protelomerase. Protelomerase resolves a concatenated dimer of chromosomes as the last step of chromosome replication, converting a palindromic DNA sequence at the junctions between chromosomes into covalently closed hairpins. The mechanism by which protelomerase transforms a duplex DNA substrate into the hairpin telomeres remains largely unknown. We report here a series of crystal structures of the protelomerase TelA bound to DNA that represent distinct stages along the reaction pathway. The structures suggest that TelA converts a linear duplex substrate into hairpin turns via a transient strand-refolding intermediate that involves DNA-base flipping and wobble base-pairs. The extremely compact di-nucleotide hairpin structure of the product is fully stabilized by TelA prior to strand ligation, which drives the reaction to completion. The enzyme-catalyzed, multistep strand refolding is a novel mechanism in DNA rearrangement reactions.

PubMed: 23382649
DOI: 10.1371/journal.pbio.1001472

Experimental method

X-RAY DIFFRACTION (2.42 Å)