1L8Q
CRYSTAL STRUCTURE OF DNA REPLICATION INITIATION FACTOR
1L8Q の概要
| エントリーDOI | 10.2210/pdb1l8q/pdb |
| 分子名称 | Chromosomal replication initiator protein dnaA, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| 機能のキーワード | aaa+, helix-turn-helix, nucleotide-binding, dna binding, replication initiation, dna binding protein |
| 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 | 1 |
| 化学式量合計 | 38501.07 |
| 構造登録者 | Erzberger, J.P.,Pirruccello, M.M.,Berger, J.M. (登録日: 2002-03-21, 公開日: 2002-09-25, 最終更新日: 2024-11-13) |
| 主引用文献 | Erzberger, J.P.,Pirruccello, M.M.,Berger, J.M. The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation Embo J., 21:4763-4773, 2002 Cited by PubMed Abstract: The initiation of DNA replication is a key event in the cell cycle of all organisms. In bacteria, replication initiation occurs at specific origin sequences that are recognized and processed by an oligomeric complex of the initiator protein DnaA. We have determined the structure of the conserved core of the Aquifex aeolicus DnaA protein to 2.7 A resolution. The protein comprises an AAA+ nucleotide-binding fold linked through a long, helical connector to an all-helical DNA-binding domain. The structure serves as a template for understanding the physical consequences of a variety of DnaA mutations, and conserved motifs in the protein suggest how two critical aspects of origin processing, DNA binding and homo-oligomerization, are mediated. The spatial arrangement of these motifs in DnaA is similar to that of the eukaryotic-like archaeal replication initiation factor Cdc6/Orc1, demonstrating that mechanistic elements of origin processing may be conserved across bacterial, archaeal and eukaryotic domains of life. PubMed: 12234917DOI: 10.1093/emboj/cdf496 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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