spacer
spacer

PDBsum entry 2m3k

Go to PDB code: 
Top Page protein links
Motor protein PDB id
2m3k
Contents
Protein chain
119 a.a.

References listed in PDB file
Key reference
Title Specific DNA recognition mediated by a type IV pilin.
Authors A.Cehovin, P.J.Simpson, M.A.Mcdowell, D.R.Brown, R.Noschese, M.Pallett, J.Brady, G.S.Baldwin, S.M.Lea, S.J.Matthews, V.Pelicic.
Ref. Proc Natl Acad Sci U S A, 2013, 110, 3065-3070. [DOI no: 10.1073/pnas.1218832110]
PubMed id 23386723
Note: In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above have been manually determined.
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.
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer