Document Detail


The surface location of individual residues in a bacterial S-layer protein.
MedLine Citation:
PMID:  18262545     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Bacterial surface layer (S-layer) proteins self-assemble into large two-dimensional crystalline lattices that form the outermost cell-wall component of all archaea and many eubacteria. Despite being a large class of self-assembling proteins, little is known about their molecular architecture. We investigated the S-layer protein SbsB from Geobacillus stearothermophilus PV72/p2 to identify residues located at the subunit-subunit interface and to determine the S-layer's topology. Twenty-three single cysteine mutants, which were previously mapped to the surface of the SbsB monomer, were subjected to a cross-linking screen using the photoactivatable, sulfhydryl-reactive reagent N-[4-(p-azidosalicylamido)butyl]-3'-(2'-pyridyldithio)propionamide. Gel electrophoretic analysis on the formation of cross-linked dimers indicated that 8 out of the 23 residues were located at the interface. In combination with surface accessibility data for the assembled protein, 10 residues were assigned to positions at the inner, cell-wall-facing lattice surface, while 5 residues were mapped to the outer, ambient-exposed lattice surface. In addition, the cross-linking screen identified six positions of intramolecular cross-linking within the assembled protein but not in the monomeric S-layer protein. Most likely, these intramolecular cross-links result from conformational changes upon self-assembly. The results are an important step toward the further structural elucidation of the S-layer protein via, for example, X-ray crystallography and cryo-electron microscopy. Our approach of identifying the surface location of residues is relevant to other planar supramolecular protein assemblies.
Authors:
Helen Kinns; Stefan Howorka
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-01-16
Journal Detail:
Title:  Journal of molecular biology     Volume:  377     ISSN:  1089-8638     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2008 Mar 
Date Detail:
Created Date:  2008-03-10     Completed Date:  2008-03-28     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  589-604     Citation Subset:  IM    
Affiliation:
Department of Chemistry, University College London, Christopher Ingold Building, 20 Gordon Street, London WC1H 0AJ, England, UK.
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MeSH Terms
Descriptor/Qualifier:
Bacillaceae / chemistry*,  metabolism
Bacterial Proteins / chemistry*,  isolation & purification,  metabolism*,  ultrastructure
Cross-Linking Reagents / chemistry
Cysteine / genetics,  metabolism
Diphosphonates / chemistry
Gene Expression
Membrane Proteins / chemistry*,  isolation & purification,  metabolism*,  ultrastructure
Microscopy, Electron, Transmission
Mutation / genetics
Recombinant Proteins / chemistry,  genetics,  isolation & purification,  metabolism
Grant Support
ID/Acronym/Agency:
//Biotechnology and Biological Sciences Research Council
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Cross-Linking Reagents; 0/Diphosphonates; 0/Membrane Proteins; 0/Recombinant Proteins; 52-90-4/Cysteine; 56269-44-4/azacycloheptane-2,2-diphosphonate

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