5IE9

Crystal structure of the Bacillus-conserved MazG protein, a nucleotide pyrophosphohydrolase

5IE9 の概要

• エントリーDOI: 10.2210/pdb5ie9/pdb
• 分子名称: Nucleotide pyrophosphohydrolase, MANGANESE (II) ION (2 entities in total)
• 機能のキーワード: mazg, nucleoside triphosphate pyrophosphohydrolase, hydrolase
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 48358.96

構造登録者

Kim, M.,Hong, M. (登録日: 2016-02-25, 公開日: 2016-03-30, 最終更新日: 2023-11-08)

主引用文献

Kim, M.I.,Hong, M.
Crystal structure of the Bacillus-conserved MazG protein, a nucleotide pyrophosphohydrolase.
Biochem.Biophys.Res.Commun., 472:237-242, 2016

PubMed Abstract: BA1544 from Bacillus anthracis was previously annotated as a transcription factor for the gene cluster ba1554 - ba1558, but has not been experimentally characterized. B. anthracis is an obligate pathogen causing fatal inhalational anthrax, and BA1544 is absolutely conserved in Bacillus species, including Bacillus cereus, Bacillus thuringiensis and Bacillus mycoides, with 100% sequence identity. To address the function of BA1544, we performed structural and biochemical studies, which revealed that BA1544 is a MazG protein. Thus, herein, the protein is defined as Bacillus-conserved MazG (BcMazG). Like other MazG structures, BcMazG assembles into a tetrameric architecture. Each monomer adopts a four-α-helix bundle that accommodates a metal ion using four acidic residues, and presents one putative substrate-binding site. Enzymatic characterization demonstrated that BcMazG is a nucleoside triphosphate (NTP) pyrophosphohydrolase and prefers adenosine triphosphate as a substrate among canonical NTPs. Moreover, structural comparison of BcMazG with its homologues revealed a potential regulation mechanism whereby the enzymatic activity of BcMazG is regulated by its C-terminal region.

PubMed: 26920050
DOI: 10.1016/j.bbrc.2016.02.097

実験手法

X-RAY DIFFRACTION (2.8 Å)