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Article

Structural and Biochemical Insight into the Mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP Phosphodiesterase.

The Journal of biological chemistry - 12 Feb 2016

He Qing, Wang Feng, Liu Shiheng, Zhu Deyu, Cong Hengjiang, Gao Fei, Li Bingqing, Wang Hongwei, Lin Zong, Liao Jun, Gu Lichuan

Abstract excerpt

The intracellular infections of Mycobacterium tuberculosis, which is the causative agent of tuberculosis, are regulated by many cyclic dinucleotide signaling. Rv2837c from M. tuberculosis is a soluble, stand-alone DHH-DHHA1 domain phosphodiesterase that down-regulates c-di-AMP through catalytic degradation and plays an important role in M. tuberculosis infections. Here, we report the crystal structure of Rv2837c...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 26668313
DOI: 10.1074/jbc.M115.699801
PMCID: PMC4751404

Genes

DHH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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