PDBsum entry 6p5t

Membrane protein

PDB id: 6p5t

Contents

Protein chains

(+ 0 more) 782 a.a.

Metals

_SR ×124

IOD ×150

Waters ×4837

PDB id:

6p5t

Name:

Membrane protein

Title:

Surface-layer (s-layer) rsaa protein from caulobacter crescentus bound to strontium and iodide

Structure:

S-layer protein. Chain: a, b, c, d, e, f. Synonym: paracrystalline surface layer protein. Engineered: yes

Source:

Caulobacter vibrioides. Organism_taxid: 155892. Gene: rsaa, cc_1007. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.10Å R-factor: 0.207 R-free: 0.243

Authors:

A.C.Chan,J.Herrmann,J.Smit,S.Wakatsuki,M.E.Murphy

Key ref:

J.Herrmann et al. (2020). A bacterial surface layer protein exploits multistep crystallization for rapid self-assembly. Proc Natl Acad Sci U S A, 117, 388-394. PubMed id: 31848245 DOI: 10.1073/pnas.1909798116

Date:

30-May-19 Release date: 15-Jan-20

Protein chains

P35828  (SLAP_CAUVC) -  S-layer protein from Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)

Seq: 1026 a.a.

Struc: 782 a.a.

DOI no: 10.1073/pnas.1909798116

Proc Natl Acad Sci U S A 117:388-394 (2020)

PubMed id: 31848245

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

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.

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.