The full-length Streptococcus pneumoniae major pilin RrgB crystallizes in a fibre-like structure, which presents the D1 isopeptide bond and provides details on the mechanism of pilus polymerization

The full-length Streptococcus pneumoniae major pilin RrgB crystallizes in a fibre-like structure, which presents the D1 isopeptide bond and provides details on the mechanism of pilus polymerization

Item
http://www.wikidata.org/entity/Q27675142
Pilins in gram-positive bacteria: A structural perspectiveThe Pilin Protein FimP from Actinomyces oris: Crystal Structure and Sequence AnalysesIsopeptide bonds of the major pilin protein BcpA influence pilus structure and bundle formation on the surface of Bacillus cereusStructural Basis of Pilus Anchoring by the Ancillary Pilin RrgC of Streptococcus pneumoniaeStructural Conservation, Variability, and Immunogenicity of the T6 Backbone Pilin of Serotype M6 Streptococcus pyogenesA slow-forming isopeptide bond in the structure of the major pilin SpaD fromCorynebacterium diphtheriaehas implications for pilus assemblyProtective activity of the CnaBE3 domain conserved among Staphylococcus aureus Sdr proteins.Structure and assembly of group B streptococcus pilus 2b backbone protein.A structural snapshot of type II pilus formation in Streptococcus pneumoniaeNew insights about pilus formation in gut-adapted Lactobacillus rhamnosus GG from the crystal structure of the SpaA backbone-pilin subunit.Pilin and sortase residues critical for endocarditis- and biofilm-associated pilus biogenesis in Enterococcus faecalisPilus biogenesis of Gram-positive bacteria: Roles of sortases and implications for assembly.Engineering a Lys-Asn isopeptide bond into an immunoglobulin-like protein domain enhances its stability.Autocatalytic association of proteins by covalent bond formation: a Bio Molecular Welding toolbox derived from a bacterial adhesinBent conformation of a backbone pilin N-terminal domain supports a three-stage pilus assembly mechanism
P2860

The full-length Streptococcus pneumoniae major pilin RrgB crystallizes in a fibre-like structure, which presents the D1 isopeptide bond and provides details on the mechanism of pilus polymerization

Item
http://www.wikidata.org/entity/Q27675142
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2012 nî lūn-bûn
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2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած
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2012 թվականի փետրվարին հրատարակված գիտական հոդված
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2012年の論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年论文
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name
The full-length Streptococcus ...... hanism of pilus polymerization
@ast
The full-length Streptococcus ...... hanism of pilus polymerization
@en
The full-length Streptococcus ...... hanism of pilus polymerization
@nl
type
label
The full-length Streptococcus ...... hanism of pilus polymerization
@ast
The full-length Streptococcus ...... hanism of pilus polymerization
@en
The full-length Streptococcus ...... hanism of pilus polymerization
@nl
prefLabel
The full-length Streptococcus ...... hanism of pilus polymerization
@ast
The full-length Streptococcus ...... hanism of pilus polymerization
@en
The full-length Streptococcus ...... hanism of pilus polymerization
@nl
P1433
P1476
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P5875
P698
P3181
P356
P1433
P1476
The full-length Streptococcus ...... hanism of pilus polymerization
@en
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P5875
P698