1BF8

PERIPLASMIC CHAPERONE FIMC, NMR, 20 STRUCTURES

Summary for 1BF8

• Entry DOI: 10.2210/pdb1bf8/pdb
• Descriptor: CHAPERONE PROTEIN FIMC (1 entity in total)
• Functional Keywords: chaperone, fimc, periplasmic chaperone, pilus chaperone, type-i pili
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 22754.03

Authors

Pellecchia, M.,Guntert, P.,Glockshuber, R.,Wuthrich, K. (deposition date: 1998-05-28, release date: 1998-11-18, Last modification date: 2024-05-22)

Primary citation

Pellecchia, M.,Guntert, P.,Glockshuber, R.,Wuthrich, K.
NMR solution structure of the periplasmic chaperone FimC.
Nat.Struct.Biol., 5:885-890, 1998

PubMed Abstract: 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.

PubMed: 9783748
DOI: 10.1038/2325

Experimental method

SOLUTION NMR