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PDBsum entry 5vba
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Chaperone, hydrolase
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PDB id
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5vba
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References listed in PDB file
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Key reference
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Title
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Structural variability of espg chaperones from mycobacterial esx-1, Esx-3, And esx-5 type VII secretion systems.
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Authors
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A.T.Tuukkanen,
D.Freire,
S.Chan,
M.A.Arbing,
R.W.Reed,
T.J.Evans,
G.Zenkeviciutė,
J.Kim,
S.Kahng,
M.R.Sawaya,
C.T.Chaton,
M.Wilmanns,
D.Eisenberg,
A.H.A.Parret,
K.V.Korotkov.
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Ref.
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J Mol Biol, 2019,
431,
289-307.
[DOI no: ]
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PubMed id
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Abstract
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Type VII secretion systems (ESX) are responsible for transport of multiple
proteins in mycobacteria. How different ESX systems achieve specific secretion
of cognate substrates remains elusive. In the ESX systems, the cytoplasmic
chaperone EspG forms complexes with heterodimeric PE-PPE substrates that are
secreted from the cells or remain associated with the cell surface. Here we
report the crystal structure of the EspG1 chaperone from the ESX-1
system determined using a fusion strategy with T4 lysozyme. EspG1
adopts a quasi 2-fold symmetric structure that consists of a central β-sheet
and two α-helical bundles. In addition, we describe the structures of
EspG3 chaperones from four different crystal forms. Alternate
conformations of the putative PE-PPE binding site are revealed by comparison of
the available EspG3 structures. Analysis of EspG1,
EspG3, and EspG5 chaperones using small-angle X-ray
scattering reveals that EspG1 and EspG3 chaperones form
dimers in solution, which we observed in several of our crystal forms. Finally,
we propose a model of the ESX-3 specific EspG3-PE5-PPE4 complex based
on the small-angle X-ray scattering analysis.
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