Type-4 pilus-structure: outside to inside and top to bottom--a minireview.
We have recently proposed a computational model of the N. gonorrhoeae pilus fiber based on the high resolution X-ray crystal structure of the component protein pilin, combined with available biophysical and genetic data [Parge et al. (1995) Nature 378, 32-38]. In parallel, we have used anti-peptide antibodies to distinguish buried and exposed regions of pilin within the assembled fiber [Forest et al. (1996) Infect. Immun. 64, 644-652]. This mini-review addresses the properties of the current pilus model and the locations of end-exposed epitopes. The fiber forms a three-layered structure of coiled conserved alpha helices surrounded by beta-sheet, with the hypervariable region as the most highly exposed portion. Overall the pilus model developed from diffraction and antibody mapping is expected to be representative of type-4 pili with general implications for type-4 assembly, function, and interactions with other proteins and cell membranes.
Forest
K T
KT
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Tainer
J A
JA
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009344:Neisseria gonorrhoeae / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D001425:Bacterial Outer Membrane Proteins; D036781:Fimbriae Proteins