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PDBsum entry 6p5t
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Membrane protein
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PDB id
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6p5t
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References listed in PDB file
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Key reference
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Title
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A bacterial surface layer protein exploits multistep crystallization for rapid self-Assembly.
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Authors
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J.Herrmann,
P.N.Li,
F.Jabbarpour,
A.C.K.Chan,
I.Rajkovic,
T.Matsui,
L.Shapiro,
J.Smit,
T.M.Weiss,
M.E.P.Murphy,
S.Wakatsuki.
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Ref.
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Proc Natl Acad Sci U S A, 2020,
117,
388-394.
[DOI no: ]
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PubMed id
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Abstract
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Surface layers (S-layers) are crystalline protein coats surrounding microbial
cells. S-layer proteins (SLPs) regulate their extracellular self-assembly by
crystallizing when exposed to an environmental trigger. However, molecular
mechanisms governing rapid protein crystallization in vivo or in vitro are
largely unknown. Here, we demonstrate that the Caulobacter crescentus SLP
readily crystallizes into sheets in vitro via a calcium-triggered multistep
assembly pathway. This pathway involves 2 domains serving distinct functions in
assembly. The C-terminal crystallization domain forms the physiological
2-dimensional (2D) crystal lattice, but full-length protein crystallizes
multiple orders of magnitude faster due to the N-terminal nucleation domain.
Observing crystallization using a time course of electron cryo-microscopy
(Cryo-EM) imaging reveals a crystalline intermediate wherein N-terminal
nucleation domains exhibit motional dynamics with respect to rigid
lattice-forming crystallization domains. Dynamic flexibility between the 2
domains rationalizes efficient S-layer crystal nucleation on the curved cellular
surface. Rate enhancement of protein crystallization by a discrete nucleation
domain may enable engineering of kinetically controllable self-assembling 2D
macromolecular nanomaterials.
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