1HPW

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

1HPW の概要

• エントリーDOI: 10.2210/pdb1hpw/pdb
• 分子名称: FIMBRIAL PROTEIN (1 entity in total)
• 機能のキーワード: fimbria, methylation, contractile protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13116.64

構造登録者

Keizer, D.W.,Slupsky, C.M.,Campbell, A.P.,Irvin, R.T.,Sykes, B.D. (登録日: 2000-12-13, 公開日: 2001-05-02, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

SOLUTION NMR