Structural and Biochemical Insight into the Mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP Phosphodiesterase
He, Qing1; Wang, Feng1; Liu, Shiheng1; Zhu, Deyu1; Cong, Hengjiang1; Gao, Fei1; Li, Bingqing1; Wang, Hongwei1; Lin, Zong2; Liao, Jun3; Gu, Lichuan1
2016-02-12
Source PublicationJOURNAL OF BIOLOGICAL CHEMISTRY
ISSN0021-9258
Volume291Issue:7Pages:3668-3681
Status已发表
DOI10.1074/jbc.M115.699801
AbstractThe 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 (2.0 angstrom), and its complex with hydrolysis intermediate 5-pApA (2.35 angstrom). Our structures indicate that both DHH and DHHA1 domains are essential for c-di-AMP degradation. Further structural analysis shows that Rv2837c does not distinguish adenine from guanine, which explains why Rv2837c hydrolyzes all linear dinucleotides with almost the same efficiency. We observed that Rv2837c degraded other c-di-NMPs at a lower rate than it did on c-di-AMP. Nevertheless, our data also showed that Rv2837c significantly decreases concentrations of both c-di-AMP and c-di-GMP in vivo. Our results suggest that beside its major role in c-di-AMP degradation Rv2837c could also regulate c-di-GMP signaling pathways in bacterial cell.
Keywordcyclic diadenosine monophosphate (c-di-AMP) enzyme degradation Mycobacterium tuberculosis phosphodiesterases structure-function
Indexed BySCI ; EI
Language英语
Funding ProjectZhejiang Natural Science Foundation[LR12C05001]
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
WOS IDWOS:000370854500044
PublisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
EI Accession Number20161802327247
EI KeywordsCrystal structure ; Esters ; Tubes (components)
EI Classification NumberBiomedical Engineering:461.1 ; Pipe, Piping and Pipelines:619.1 ; Organic Compounds:804.1 ; Crystal Lattice:933.1.1
WOS KeywordAFFECT BACTERIAL-GROWTH ; LONG-TERM SURVIVAL ; AMP PHOSPHODIESTERASE ; GMP ; IDENTIFICATION ; SPORULATION ; RESOLUTION ; REVEALS ; PROTEIN ; LEADS
Original Document TypeArticle
Citation statistics
Cited Times:31[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttps://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1924
Collection生命科学与技术学院_PI研究组_廖军组
Corresponding AuthorGu, Lichuan
Affiliation1.Shandong Univ, Sch Life Sci, State Key Lab Microbial Technol, Jinan 250100, Shandong, Peoples R China
2.Tsinghua Univ, Yangtze Delta Reg Inst, Dept Biotechnol & Biomed, Jiaxing 314006, Zhejiang, Peoples R China
3.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 200031, Peoples R China
Recommended Citation
GB/T 7714
He, Qing,Wang, Feng,Liu, Shiheng,et al. Structural and Biochemical Insight into the Mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP Phosphodiesterase[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2016,291(7):3668-3681.
APA He, Qing.,Wang, Feng.,Liu, Shiheng.,Zhu, Deyu.,Cong, Hengjiang.,...&Gu, Lichuan.(2016).Structural and Biochemical Insight into the Mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP Phosphodiesterase.JOURNAL OF BIOLOGICAL CHEMISTRY,291(7),3668-3681.
MLA He, Qing,et al."Structural and Biochemical Insight into the Mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP Phosphodiesterase".JOURNAL OF BIOLOGICAL CHEMISTRY 291.7(2016):3668-3681.
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