5IE9

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

Summary for 5IE9

• Entry DOI: 10.2210/pdb5ie9/pdb
• Descriptor: Nucleotide pyrophosphohydrolase, MANGANESE (II) ION (2 entities in total)
• Functional Keywords: mazg, nucleoside triphosphate pyrophosphohydrolase, hydrolase
• Biological source: Bacillus cereus
• Total number of polymer chains: 4
• Total formula weight: 48358.96

Authors

Kim, M.,Hong, M. (deposition date: 2016-02-25, release date: 2016-03-30, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)