|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5430
|
|
pubmed:dateCreated |
1999-9-2
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Many Gram-negative pathogens assemble architecturally and functionally diverse adhesive pili on their surfaces by the chaperone-usher pathway. Immunoglobulin-like periplasmic chaperones escort pilus subunits to the usher, a large protein complex that facilitates the translocation and assembly of subunits across the outer membrane. The crystal structure of the PapD-PapK chaperone-subunit complex, determined at 2.4 angstrom resolution, reveals that the chaperone functions by donating its G(1) beta strand to complete the immunoglobulin-like fold of the subunit via a mechanism termed donor strand complementation. The structure of the PapD-PapK complex also suggests that during pilus biogenesis, every subunit completes the immunoglobulin-like fold of its neighboring subunit via a mechanism termed donor strand exchange.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
0036-8075
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
13
|
|
pubmed:volume |
285
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1058-61
|
|
pubmed:dateRevised |
2007-11-14
|
|
pubmed:meshHeading |
pubmed-meshheading:10446050-Amino Acid Sequence,
pubmed-meshheading:10446050-Bacterial Proteins,
pubmed-meshheading:10446050-Crystallography, X-Ray,
pubmed-meshheading:10446050-Escherichia coli,
pubmed-meshheading:10446050-Escherichia coli Proteins,
pubmed-meshheading:10446050-Fimbriae, Bacterial,
pubmed-meshheading:10446050-Fimbriae Proteins,
pubmed-meshheading:10446050-Models, Molecular,
pubmed-meshheading:10446050-Molecular Chaperones,
pubmed-meshheading:10446050-Molecular Sequence Data,
pubmed-meshheading:10446050-Periplasmic Proteins,
pubmed-meshheading:10446050-Protein Conformation,
pubmed-meshheading:10446050-Protein Folding,
pubmed-meshheading:10446050-Protein Structure, Secondary,
pubmed-meshheading:10446050-Sequence Alignment
|
|
pubmed:year |
1999
|
|
pubmed:articleTitle |
Structural basis of chaperone function and pilus biogenesis.
|
|
pubmed:affiliation |
Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|
