1HPW

STRUCTURE OF A PILIN MONOMER FROM PSEUDOMONAS AERUGINOSA: IMPLICATIONS FOR THE ASSEMBLY OF PILI.

Summary for 1HPW

• Entry DOI: 10.2210/pdb1hpw/pdb
• Descriptor: FIMBRIAL PROTEIN (1 entity in total)
• Functional Keywords: fimbria, methylation, contractile protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 13116.64

Authors

Keizer, D.W.,Slupsky, C.M.,Campbell, A.P.,Irvin, R.T.,Sykes, B.D. (deposition date: 2000-12-13, release date: 2001-05-02, Last modification date: 2024-10-30)

Primary citation

Keizer, D.W.,Slupsky, C.M.,Kalisiak, M.,Campbell, A.P.,Crump, M.P.,Sastry, P.A.,Hazes, B.,Irvin, R.T.,Sykes, B.D.
Structure of a pilin monomer from Pseudomonas aeruginosa: implications for the assembly of pili.
J.Biol.Chem., 276:24186-24193, 2001

PubMed Abstract: Type IV pilin monomers assemble to form fibers called pili that are required for a variety of bacterial functions. Pilin monomers oligomerize due to the interaction of part of their hydrophobic N-terminal alpha-helix. Engineering of a truncated pilin from Pseudomonas aeruginosa strain K122-4, where the first 28 residues are removed from the N terminus, yields a soluble, monomeric protein. This truncated pilin is shown to bind to its receptor and to decrease morbidity and mortality in mice upon administration 15 min before challenge with a heterologous strain of Pseudomonas. The structure of this truncated pilin reveals an alpha-helix at the N terminus that lies across a 4-stranded antiparallel beta-sheet. A model for a pilus is proposed that takes into account both electrostatic and hydrophobic interactions of pilin subunits as well as previously published x-ray fiber diffraction data. Our model indicates that DNA or RNA cannot pass through the center of the pilus, however, the possibility exists for small organic molecules to pass through indicating a potential mechanism for signal transduction.

PubMed: 11294863
DOI: 10.1074/jbc.M100659200

Experimental method

SOLUTION NMR