4E10
Protelomerase tela Y201A covalently complexed with substrate DNA
Summary for 4E10
Entry DOI | 10.2210/pdb4e10/pdb |
Related | 4DWP 4E0G 4E0J 4E0P 4E0Y 4E0Z |
Descriptor | Protelomerase, DNA (5'-D(*CP*AP*TP*AP*AP*(BRU)P*AP*AP*CP*AP*AP*(BRU)P*AP*T)-3'), DNA (5'-D(*CP*AP*TP*GP*AP*TP*AP*(BRU)P*(BRU)P*GP*(BRU)P*(BRU)P*AP*(BRU)P*(BRU)P*AP*(BRU)P*G)-3'), ... (5 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 | 63014.23 |
Authors | Shi, K.,Aihara, H. (deposition date: 2012-03-05, release date: 2013-02-13, Last modification date: 2025-02-12) |
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 Cited by 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: 23382649DOI: 10.1371/journal.pbio.1001472 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.506 Å) |
Structure validation
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