6HZ7

Structure of McrBC without DNA binding domains (Class 3)

6HZ7 の概要

• エントリーDOI: 10.2210/pdb6hz7/pdb
• EMDBエントリー: 0313
• 分子名称: 5-methylcytosine-specific restriction enzyme B, Protein McrC, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total)
• 機能のキーワード: aaa+ superfamily, restriction enzyme, dna binding protein
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 516327.37

構造登録者

Itoh, Y.,Nirwan, N.,Saikrishnan, K.,Amunts, A. (登録日: 2018-10-22, 公開日: 2019-07-24, 最終更新日: 2024-05-15)

主引用文献

Nirwan, N.,Itoh, Y.,Singh, P.,Bandyopadhyay, S.,Vinothkumar, K.R.,Amunts, A.,Saikrishnan, K.
Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC.
Nat Commun, 10:3058-3058, 2019

PubMed Abstract: The AAA+ GTPase McrB powers DNA cleavage by the endonuclease McrC. The GTPase itself is activated by McrC. The architecture of the GTPase and nuclease complex, and the mechanism of their activation remained unknown. Here, we report a 3.6 Å structure of a GTPase-active and DNA-binding deficient construct of McrBC. Two hexameric rings of McrB are bridged by McrC dimer. McrC interacts asymmetrically with McrB protomers and inserts a stalk into the pore of the ring, reminiscent of the γ subunit complexed to αβ of F-ATPase. Activation of the GTPase involves conformational changes of residues essential for hydrolysis. Three consecutive nucleotide-binding pockets are occupied by the GTP analogue 5'-guanylyl imidodiphosphate and the next three by GDP, which is suggestive of sequential GTP hydrolysis.

PubMed: 31296862
DOI: 10.1038/s41467-019-11084-1

実験手法

ELECTRON MICROSCOPY (4.3 Å)