3R8F
Replication initiator DnaA bound to AMPPCP and single-stranded DNA
3R8F の概要
| エントリーDOI | 10.2210/pdb3r8f/pdb |
| 分子名称 | Chromosomal replication initiator protein dnaA, 5'-D(P*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*A)-3', MAGNESIUM ION, ... (5 entities in total) |
| 機能のキーワード | aaa+ atpase, replication initiator, dna binding, replication activator-dna complex, replication activator/dna |
| 由来する生物種 | Aquifex aeolicus |
| 細胞内の位置 | Cytoplasm: O66659 |
| タンパク質・核酸の鎖数 | 5 |
| 化学式量合計 | 157279.51 |
| 構造登録者 | |
| 主引用文献 | Duderstadt, K.E.,Chuang, K.,Berger, J.M. DNA stretching by bacterial initiators promotes replication origin opening. Nature, 478:209-213, 2011 Cited by PubMed Abstract: Many replication initiators form higher-order oligomers that process host replication origins to promote replisome formation. In addition to dedicated duplex-DNA-binding domains, cellular initiators possess AAA+ (ATPases associated with various cellular activities) elements that drive functions ranging from protein assembly to origin recognition. In bacteria, the AAA+ domain of the initiator DnaA has been proposed to assist in single-stranded DNA formation during origin melting. Here we show crystallographically and in solution that the ATP-dependent assembly of Aquifex aeolicus DnaA into a spiral oligomer creates a continuous surface that allows successive AAA+ domains to bind and extend single-stranded DNA segments. The mechanism of binding is unexpectedly similar to that of RecA, a homologous recombination factor, but it differs in that DnaA promotes a nucleic acid conformation that prevents pairing of a complementary strand. These findings, combined with strand-displacement assays, indicate that DnaA opens replication origins by a direct ATP-dependent stretching mechanism. Comparative studies reveal notable commonalities between the approach used by DnaA to engage DNA substrates and other, nucleic-acid-dependent, AAA+ systems. PubMed: 21964332DOI: 10.1038/nature10455 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.366 Å) |
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