2M3K

Global fold of the type IV pilin ComP from Neisseria meningitidis

Summary for 2M3K

• Entry DOI: 10.2210/pdb2m3k/pdb
• NMR Information: BMRB: 18966
• Descriptor: Minor pilin ComP (1 entity in total)
• Functional Keywords: dna uptake, motor protein
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 1
• Total formula weight: 13512.77

Authors

Simpson, P. (deposition date: 2013-01-21, release date: 2013-02-13, Last modification date: 2024-10-16)

Primary citation

Cehovin, A.,Simpson, P.J.,McDowell, M.A.,Brown, D.R.,Noschese, R.,Pallett, M.,Brady, J.,Baldwin, G.S.,Lea, S.M.,Matthews, S.J.,Pelicic, V.
Specific DNA recognition mediated by a type IV pilin.
Proc.Natl.Acad.Sci.USA, 110:3065-3070, 2013

PubMed Abstract: Natural transformation is a dominant force in bacterial evolution by promoting horizontal gene transfer. This process may have devastating consequences, such as the spread of antibiotic resistance or the emergence of highly virulent clones. However, uptake and recombination of foreign DNA are most often deleterious to competent species. Therefore, model naturally transformable gram-negative bacteria, including the human pathogen Neisseria meningitidis, have evolved means to preferentially take up homotypic DNA containing short and genus-specific sequence motifs. Despite decades of intense investigations, the DNA uptake sequence receptor in Neisseria species has remained elusive. We show here, using a multidisciplinary approach combining biochemistry, molecular genetics, and structural biology, that meningococcal type IV pili bind DNA through the minor pilin ComP via an electropositive stripe that is predicted to be exposed on the filaments surface and that ComP displays an exquisite binding preference for DNA uptake sequence. Our findings illuminate the earliest step in natural transformation, reveal an unconventional mechanism for DNA binding, and suggest that selective DNA uptake is more widespread than previously thought.

PubMed: 23386723
DOI: 10.1073/pnas.1218832110

Experimental method

SOLUTION NMR