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A bacterial surface layer protein exploits multistep crystallization for rapid self-assembly.


ABSTRACT: 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.

SUBMITTER: Herrmann J 

PROVIDER: S-EPMC6955313 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature

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A bacterial surface layer protein exploits multistep crystallization for rapid self-assembly.

Herrmann Jonathan J   Li Po-Nan PN   Jabbarpour Fatemeh F   Chan Anson C K ACK   Rajkovic Ivan I   Matsui Tsutomu T   Shapiro Lucy L   Smit John J   Weiss Thomas M TM   Murphy Michael E P MEP   Wakatsuki Soichi S  

Proceedings of the National Academy of Sciences of the United States of America 20191217 1


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 <i>Caulobacter crescentus</i> SLP readily crystallizes into sheets in vitro via a calcium-triggered multistep assembly pathway. This pathway involve  ...[more]

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