Document Detail


Structure and assembly of Yersinia pestis F1 antigen.
MedLine Citation:
PMID:  17966405     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Most Gram negative pathogens express surface located fibrillar organelles that are used for adhesion to host epithelia and/or for protection. The assembly of many such organelles is managed by a highly conserved periplasmic chaperone/usher assembly pathway. During the last few years, considerable progress has been made in understanding how periplasmic chaperones mediate folding, targeting, and assembly of F1 antigen subunits into the F1 capsular antigen. In particular, structures representing snapshots of several of the steps involved in assembly have allowed us to begin to draw a detailed molecular-level picture of F1 assembly specifically, and of chaperone/usher-mediated assembly in general. Here, a brief summary of these new results will be presented.
Authors:
Stefan D Knight
Related Documents :
10394365 - The crystal structure of the human hepatitis b virus capsid.
10545185 - Identification and characterization of the domain structure of bacteriophage p22 coat p...
18814295 - Thermostability and molecular encapsulation within an engineered caged protein scaffold.
1557405 - Nucleoplasmic localization of prelamin a: implications for prenylation-dependent lamin ...
11276255 - A universal mode of helix packing in rna.
10205635 - Effect of penetration enhancers on the permeation of the thyrotropin releasing hormone ...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Advances in experimental medicine and biology     Volume:  603     ISSN:  0065-2598     ISO Abbreviation:  Adv. Exp. Med. Biol.     Publication Date:  2007  
Date Detail:
Created Date:  2007-10-26     Completed Date:  2007-12-07     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0121103     Medline TA:  Adv Exp Med Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  74-87     Citation Subset:  IM    
Affiliation:
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala. Knight@molbio.slu.se
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Antigens, Bacterial / chemistry*,  metabolism*
Bacterial Proteins / chemistry*,  immunology,  metabolism*
Fimbriae Proteins / chemistry,  immunology,  metabolism
Fimbriae, Bacterial / metabolism,  ultrastructure
Models, Biological
Models, Molecular
Molecular Chaperones / chemistry,  metabolism
Multiprotein Complexes
Protein Folding
Protein Structure, Quaternary
Protein Subunits
Thermodynamics
Yersinia pestis / immunology*,  metabolism,  ultrastructure
Chemical
Reg. No./Substance:
0/Antigens, Bacterial; 0/Bacterial Proteins; 0/Molecular Chaperones; 0/Multiprotein Complexes; 0/Protein Subunits; 0/caf1 protein, Yersinia pestis; 141911-75-3/CAf1M protein, Yersinia pestis; 147680-16-8/Fimbriae Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  My life with Yersinia.
Next Document:  Relationship of the lipopolysaccharide structure of Yersinia pestis to resistance to antimicrobial f...