Under construction. Last update March 28 1995
PapD: P-pilus chaperone (E. coli)
PapD
The structure of PapD was solved by Holmgren &
Branden (1989) . Click here to see a
picture of the PapD molecule. Residues at the bottom of the subunit
binding cleft are highly conserved throughout the family of periplasmic
pilus chaperones. In particular, residues in two rows on the inner beta-sheet
of the N-terminal domain are highly conserved and important for chaperone
function. If you would like to see a closeup of these rows, click
here .
Stefan Knight
Swedish University of Agricultural Sciences
Uppsala Biomedical Centre
Department of Molecular Biology
P.O. Box 590
S-751 24 Uppsala
Sweden
stefan@xray.bmc.uu.se
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