SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly

被引:113
作者
Baranova, Ekaterina [1 ,2 ]
Fronzes, Remi [3 ,4 ]
Garcia-Pino, Abel [2 ]
Van Gerven, Nani [1 ,2 ]
Papapostolou, David [5 ]
Pehau-Arnaudet, Gerard [4 ]
Pardon, Els [2 ]
Steyaert, Jan [2 ]
Howorka, Stefan [5 ]
Remaut, Han [1 ,2 ]
机构
[1] VIB, VIB Dept Struct Biol, B-1050 Brussels, Belgium
[2] Vrije Univ Brussel, B-1050 Brussels, Belgium
[3] Inst Pasteur, Unite G5, F-75015 Paris, France
[4] Inst Pasteur, CNRS, Unite Rech Mixte 3538, F-75015 Paris, France
[5] UCL, Inst Struct & Mol Biol, Dept Chem, London WC1H 0AJ, England
基金
英国生物技术与生命科学研究理事会;
关键词
PROTEIN SBSB; DOMAINS; BINDING; SYSTEM; ORGANIZATION; SCATTERING; ANTHRACIS; RESIDUES; ADHESION; MODEL;
D O I
10.1038/nature11155
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
S-layers are regular two-dimensional semipermeable protein layers that constitute a major cell-wall component in archaea and many bacteria(1-3). The nanoscale repeat structure of the S-layer lattices and their self-assembly from S-layer proteins (SLPs) have sparked interest in their use as patterning and display scaffolds for a range of nano-biotechnological applications(4-7). Despite their biological abundance and the technological interest in them, structural information about SLPs is limited to truncated and assembly-negative proteins(8-10). Here we report the X-ray structure of the SbsB SLP of Geobacillus stearothermophilus PV72/p2 by the use of nanobody-aided crystallization. SbsB consists of a seven-domain protein, formed by an amino-terminal cell-wall attachment domain and six consecutive immunoglobulin-like domains, that organize into a phi-shaped disk-like monomeric crystallization unit stabilized by interdomain Ca2+ ion coordination. A Ca2+-dependent switch to the condensed SbsB quaternary structure pre-positions intermolecular contact zones and renders the protein competent for S-layer assembly. On the basis of crystal packing, chemical crosslinking data and cryo-electron microscopy projections, we present a model for the molecular organization of this SLP into a porous protein sheet inside the S-layer. The SbsB lattice represents a previously undescribed structural model for protein assemblies and may advance our understanding of SLP physiology and self-assembly, as well as the rational design of engineered higher-order structures for biotechnology(4-7).
引用
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页码:119 / +
页数:6
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