5W35

Crystal structure of the RNA polymerase domain (RPD) of Mycobacterium tuberculosis primase DnaG in complex with a double-stranded DNA oligomer with a 1-nucleotide overhang

5W35 の概要

• エントリーDOI: 10.2210/pdb5w35/pdb
• 関連するPDBエントリー: 5W33 5W34 5w36
• 分子名称: DNA primase, synthetic DNA oligomer 5'-CCACTTCCGGTC, synthetic DNA oligomer 5'-TGACCGGAAGTGG (3 entities in total)
• 機能のキーワード: dna replication, replisome, toprim fold, dna binding, transferase-dna complex, transferase/dna
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 78531.80

構造登録者

Hou, C.,Tsodikov, O.V. (登録日: 2017-06-07, 公開日: 2018-03-28, 最終更新日: 2023-10-04)

主引用文献

Hou, C.,Biswas, T.,Tsodikov, O.V.
Structures of the Catalytic Domain of Bacterial Primase DnaG in Complexes with DNA Provide Insight into Key Priming Events.
Biochemistry, 57:2084-2093, 2018

PubMed Abstract: Bacterial primase DnaG is an essential nucleic acid polymerase that generates primers for replication of chromosomal DNA. The mechanism of DnaG remains unclear due to the paucity of structural information on DnaG in complexes with other replisome components. Here we report the first crystal structures of noncovalent DnaG-DNA complexes, obtained with the RNA polymerase domain of Mycobacterium tuberculosis DnaG and various DNA ligands. One structure, obtained with ds DNA, reveals interactions with DnaG as it slides on ds DNA and suggests how DnaG binds template for primer synthesis. In another structure, DNA in the active site of DnaG mimics the primer, providing insight into mechanisms for the nucleotide transfer and DNA translocation. In conjunction with the recent cryo-EM structure of the bacteriophage T7 replisome, this study yields a model for primer elongation and hand-off to DNA polymerase.

PubMed: 29558114
DOI: 10.1021/acs.biochem.8b00036

実験手法

X-RAY DIFFRACTION (3.31 Å)