5ZMM

Structure of the Type IV phosphorothioation-dependent restriction endonuclease ScoMcrA

5ZMM の概要

• エントリーDOI: 10.2210/pdb5zmm/pdb
• 分子名称: Uncharacterized protein McrA, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: type iv restriction endonuclease, dna phosphorothioation, dna binding protein
• 由来する生物種: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 374512.72

構造登録者

Liu, G.,Fu, W.,Zhang, Z.,He, Y.,Yu, H.,Zhao, Y.,Deng, Z.,Wu, G.,He, X. (登録日: 2018-04-04, 公開日: 2018-09-26, 最終更新日: 2024-03-27)

主引用文献

Liu, G.,Fu, W.,Zhang, Z.,He, Y.,Yu, H.,Wang, Y.,Wang, X.,Zhao, Y.,Deng, Z.,Wu, G.,He, X.
Structural basis for the recognition of sulfur in phosphorothioated DNA.
Nat Commun, 9:4689-4689, 2018

PubMed Abstract: There have been very few reports on protein domains that specifically recognize sulfur. Here we present the crystal structure of the sulfur-binding domain (SBD) from the DNA phosphorothioation (PT)-dependent restriction endonuclease ScoMcrA. SBD contains a hydrophobic surface cavity that is formed by the aromatic ring of Y164, the pyrolidine ring of P165, and the non-polar side chains of four other residues that serve as lid, base, and wall of the cavity. The SBD and PT-DNA undergo conformational changes upon binding. The SRGRR loop inserts into the DNA major groove to make contacts with the bases of the GGCC core sequence. Mutating key residues of SBD impairs PT-DNA association. More than 1000 sequenced microbial species from fourteen phyla contain SBD homologs. We show that three of these homologs bind PT-DNA in vitro and restrict PT-DNA gene transfer in vivo. These results show that SBD-like PT-DNA readers exist widely in prokaryotes.

PubMed: 30409991
DOI: 10.1038/s41467-018-07093-1

実験手法

X-RAY DIFFRACTION (3.15 Å)