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- SASDD33: Toxin/Antitoxin complex from M. tuberculosis (Mycobacterial cidal... -

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Basic information

Entry
Database: SASBDB / ID: SASDD33
SampleToxin/Antitoxin complex from M. tuberculosis
  • Mycobacterial cidal toxin (protein), MbcT, Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
  • Mycobacterial cidal antitoxin (protein), MbcA, Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function / homologyAntitoxin Xre/MbcA/ParS-like, toxin-binding domain / Antitoxin Xre/MbcA/ParS C-terminal toxin-binding domain / RES domain / RES domain / RES / Transferases; Glycosyltransferases; Pentosyltransferases / nucleotidyltransferase activity / Mycobacterial cidal antitoxin MbcA / NAD(+) phosphorylase MbcT
Function and homology information
Biological speciesMycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
CitationJournal: Mol Cell / Year: 2019
Title: An NAD Phosphorylase Toxin Triggers Mycobacterium tuberculosis Cell Death.
Authors: Diana Mendes Freire / Claude Gutierrez / Acely Garza-Garcia / Anna D Grabowska / Ambre J Sala / Kanchiyaphat Ariyachaokun / Terezie Panikova / Katherine S H Beckham / André Colom / Vivian ...Authors: Diana Mendes Freire / Claude Gutierrez / Acely Garza-Garcia / Anna D Grabowska / Ambre J Sala / Kanchiyaphat Ariyachaokun / Terezie Panikova / Katherine S H Beckham / André Colom / Vivian Pogenberg / Michele Cianci / Anne Tuukkanen / Yves-Marie Boudehen / Antonio Peixoto / Laure Botella / Dmitri I Svergun / Dirk Schnappinger / Thomas R Schneider / Pierre Genevaux / Luiz Pedro Sorio de Carvalho / Matthias Wilmanns / Annabel H A Parret / Olivier Neyrolles /
Abstract: Toxin-antitoxin (TA) systems regulate fundamental cellular processes in bacteria and represent potential therapeutic targets. We report a new RES-Xre TA system in multiple human pathogens, including ...Toxin-antitoxin (TA) systems regulate fundamental cellular processes in bacteria and represent potential therapeutic targets. We report a new RES-Xre TA system in multiple human pathogens, including Mycobacterium tuberculosis. The toxin, MbcT, is bactericidal unless neutralized by its antitoxin MbcA. To investigate the mechanism, we solved the 1.8 Å-resolution crystal structure of the MbcTA complex. We found that MbcT resembles secreted NAD-dependent bacterial exotoxins, such as diphtheria toxin. Indeed, MbcT catalyzes NAD degradation in vitro and in vivo. Unexpectedly, the reaction is stimulated by inorganic phosphate, and our data reveal that MbcT is a NAD phosphorylase. In the absence of MbcA, MbcT triggers rapid M. tuberculosis cell death, which reduces mycobacterial survival in macrophages and prolongs the survival of infected mice. Our study expands the molecular activities employed by bacterial TA modules and uncovers a new class of enzymes that could be exploited to treat tuberculosis and other infectious diseases.
Contact author
  • Anne Tuukkanen (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #1743
Type: atomic / Radius of dummy atoms: 1.90 A / Chi-square value: 1.007 / P-value: 0.259841
Search similar-shape structures of this assembly by Omokage search (details)
Model #1745
Type: dummy / Radius of dummy atoms: 2.50 A / Symmetry: P1 / Chi-square value: 0.969 / P-value: 0.080559
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Toxin/Antitoxin complex from M. tuberculosis / Specimen concentration: 0.63 mg/ml / Entity id: 948 / 949
BufferName: 100 mM HEPES, 100 mM NaCl / pH: 7.5
Entity #948Name: MbcT / Type: protein / Description: Mycobacterial cidal toxin / Formula weight: 20.248 / Num. of mol.: 6
Source: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
References: UniProt: P9WLP9
Sequence:
VSDALDEGLV QRIDARGTIE WSETCYRYTG AHRDALSGEG ARRFGGRWNP PLLFPAIYLA DSAQACMVEV ERAAQAASTT AEKMLEAAYR LHTIDVTDLA VLDLTTPQAR EAVGLENDDI YGDDWSGCQA VGHAAWFLHM QGVLVPAAGG VGLVVTAYEQ RTRPGQLQLR QSVDLTPALY QELRAT
Entity #949Name: MbcA / Type: protein / Description: Mycobacterial cidal antitoxin / Formula weight: 12.616 / Num. of mol.: 6
Source: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
References: UniProt: P9WLP7
Sequence:
GAMGVNVLAS TVSGAIERLG LTYEEVGDIV DASPRSVARW TAGQVVPQRL NKQRLIELAY VADALAEVLP RDQANVWMFS PNRLLEHRKP ADLVRDGEYQ RVLALIDAMA EGVFV

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Experimental information

BeamInstrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 3 mm
DetectorName: Pilatus 2M
Scan
Title: Toxin/Antitoxin complex from M. tuberculosis / Measurement date: Jun 2, 2015 / Storage temperature: 20 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
MinMax
Q0.0983 4.8012
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 698 /
MinMax
Q0.0982867 1.93982
P(R) point1 698
R0 11.35
Result
Type of curve: single_conc
ExperimentalPorodEstimatedEstimated method
MW154 kDa154 kDa--
Volume-262 nm3285 DAMMIF

P(R)P(R) errorGuinierGuinier error
Forward scattering, I031320 114 31335.6 165.14
Radius of gyration, Rg4.09 nm0.01 4.12 nm0.07

MinMax
D-11.35
Guinier point1 82

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