This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1bf8
From Proteopedia
Revision as of 03:26, 7 August 2014 by OCA (Talk | contribs)
1bf8 is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The NMR structure of the 205-residue periplasmic chaperone FimC is presented. This protein consists of two globular domains with immunoglobulin-like folds connected by a 15-residue linker peptide. The relative orientation of the two domains is defined by hydrophobic contacts and an interdomain salt bridge. FimC mediates the assembly of type-1 pili, which are filamentous surface organelles of uropathogenic Escherichia coli strains that enable the bacteria to attach to host cell surfaces and persist in macrophages. The availability of the NMR structure of FimC provides a new basis for rational design of drugs against infections by uropathogenic bacteria.
NMR solution structure of the periplasmic chaperone FimC.,Pellecchia M, Guntert P, Glockshuber R, Wuthrich K Nat Struct Biol. 1998 Oct;5(10):885-90. PMID:9783748[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Pellecchia M, Guntert P, Glockshuber R, Wuthrich K. NMR solution structure of the periplasmic chaperone FimC. Nat Struct Biol. 1998 Oct;5(10):885-90. PMID:9783748 doi:10.1038/2325
