Structure of the Mycobacterium tuberculosis type VII secretion system chaperone EspG(5) in complex with PE25-PPE41 dimer

N. Korotkova; D. Freire; T.H. Phan; R. Ummels; C.C. Creekmore; T.J. Evans; M. Wilmanns; W. Bitter; A.H.A. Parret; E.N.G. Houben; K.V. Korotkov

doi:10.1111/mmi.12770

Structure of the Mycobacterium tuberculosis type VII secretion system chaperone EspG(5) in complex with PE25-PPE41 dimer

N. Korotkova, D. Freire, T.H. Phan, R. Ummels, C.C. Creekmore, T.J. Evans, M. Wilmanns, W. Bitter, A.H.A. Parret, E.N.G. Houben, K.V. Korotkov

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Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

The growth or virulence of Mycobacterium tuberculosis bacilli depends on homologous type VII secretion systems, ESX-1, ESX-3 and ESX-5, which export a number of protein effectors across membranes to the bacterial surface and environment. PE and PPE proteins represent two large families of highly polymorphic proteins that are secreted by these ESX systems. Recently, it was shown that these proteins require system-specific cytoplasmic chaperones for secretion. Here, we report the crystal structure of M. tuberculosisESX-5-secreted PE25-PPE41 heterodimer in complex with the cytoplasmic chaperone EspG

Original language	English
Pages (from-to)	367-382
Journal	Molecular Microbiology
Volume	94
Issue number	2
DOIs	https://doi.org/10.1111/mmi.12770
Publication status	Published - 2014

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title = "Structure of the Mycobacterium tuberculosis type VII secretion system chaperone EspG(5) in complex with PE25-PPE41 dimer",

abstract = "The growth or virulence of Mycobacterium tuberculosis bacilli depends on homologous type VII secretion systems, ESX-1, ESX-3 and ESX-5, which export a number of protein effectors across membranes to the bacterial surface and environment. PE and PPE proteins represent two large families of highly polymorphic proteins that are secreted by these ESX systems. Recently, it was shown that these proteins require system-specific cytoplasmic chaperones for secretion. Here, we report the crystal structure of M. tuberculosisESX-5-secreted PE25-PPE41 heterodimer in complex with the cytoplasmic chaperone EspG",

author = "N. Korotkova and D. Freire and T.H. Phan and R. Ummels and C.C. Creekmore and T.J. Evans and M. Wilmanns and W. Bitter and A.H.A. Parret and E.N.G. Houben and K.V. Korotkov",

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doi = "10.1111/mmi.12770",

language = "English",

volume = "94",

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journal = "Molecular Microbiology",

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T1 - Structure of the Mycobacterium tuberculosis type VII secretion system chaperone EspG(5) in complex with PE25-PPE41 dimer

AU - Korotkova, N.

AU - Freire, D.

AU - Phan, T.H.

AU - Ummels, R.

AU - Creekmore, C.C.

AU - Evans, T.J.

AU - Wilmanns, M.

AU - Bitter, W.

AU - Parret, A.H.A.

AU - Houben, E.N.G.

AU - Korotkov, K.V.

PY - 2014

Y1 - 2014

N2 - The growth or virulence of Mycobacterium tuberculosis bacilli depends on homologous type VII secretion systems, ESX-1, ESX-3 and ESX-5, which export a number of protein effectors across membranes to the bacterial surface and environment. PE and PPE proteins represent two large families of highly polymorphic proteins that are secreted by these ESX systems. Recently, it was shown that these proteins require system-specific cytoplasmic chaperones for secretion. Here, we report the crystal structure of M. tuberculosisESX-5-secreted PE25-PPE41 heterodimer in complex with the cytoplasmic chaperone EspG

AB - The growth or virulence of Mycobacterium tuberculosis bacilli depends on homologous type VII secretion systems, ESX-1, ESX-3 and ESX-5, which export a number of protein effectors across membranes to the bacterial surface and environment. PE and PPE proteins represent two large families of highly polymorphic proteins that are secreted by these ESX systems. Recently, it was shown that these proteins require system-specific cytoplasmic chaperones for secretion. Here, we report the crystal structure of M. tuberculosisESX-5-secreted PE25-PPE41 heterodimer in complex with the cytoplasmic chaperone EspG

U2 - 10.1111/mmi.12770

DO - 10.1111/mmi.12770

M3 - Article

SN - 0950-382X

VL - 94

SP - 367

EP - 382

JO - Molecular Microbiology

JF - Molecular Microbiology

IS - 2

ER -

Structure of the Mycobacterium tuberculosis type VII secretion system chaperone EspG(5) in complex with PE25-PPE41 dimer

Abstract

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