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Titolo:
STRUCTURAL POLYMORPHISM OF BACTERIAL ADHESION PILI
Autore:
BULLITT E; MAKOWSKI L;
Indirizzi:
BOSTON UNIV,SCH MED,DEPT BIOPHYS BOSTON MA 02118 FLORIDA STATE UNIV,INST MOLEC BIOPHYS TALLAHASSEE FL 32306
Titolo Testata:
Nature
fascicolo: 6510, volume: 373, anno: 1995,
pagine: 164 - 167
SICI:
0028-0836(1995)373:6510<164:SPOBAP>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
UROPATHOGENIC ESCHERICHIA-COLI; SUBUNIT; IMAGES; PROTEINS; FLAGELLA; TIP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
24
Recensione:
Indirizzi per estratti:
Citazione:
E. Bullitt e L. Makowski, "STRUCTURAL POLYMORPHISM OF BACTERIAL ADHESION PILI", Nature, 373(6510), 1995, pp. 164-167

Abstract

BACTERIAL adhesion pill are designed to bind specifically and maintain attachment of bacteria to target cells. Uropathogenic P-pili are sufficiently mechanically resilient to resist the cleansing action of urine flow that removes most other bacteria(1). P-pili are 68 Angstrom indiameter and similar to 1 mu m long(2), and are composed of similar to 1,000 copies of the principal structural protein, PapA(3). They are attached to the outer membrane by a minor structural protein, PapH(4) and are terminated by an similar to 20 Angstrom diameter fibrillus composed of PapK, PapE and PapF, which presents the host-binding adhesin PapG(5-7). The amino-acid sequences of PapA(3,8), PapE(9), and PapF(9)are similar, with highly conserved C-termini being responsible for binding to PapD(10-12), the periplasmic chaperone. Our three-dimensionalreconstruction indicates that pill are formed by the tight winding ofa much thinner structure. A structural transition allows the pilus tounravel without depolymerizing, producing a thin, extended structure five times the length of the original pilus.

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Documento generato il 05/12/20 alle ore 10:37:41