PDBsum entry 2m3k

Motor protein

PDB id: 2m3k

Contents

Protein chain

119 a.a.

PDB id:

2m3k

Name:

Motor protein

Title:

Global fold of the type iv pilin comp from neisseria meningitidis

Structure:

Minor pilin comp. Chain: a. Fragment: unp residues 35-149. Synonym: comp. Engineered: yes

Source:

Neisseria meningitidis. Organism_taxid: 487. Gene: comp, nmv_2216. Expressed in: escherichia coli. Expression_system_taxid: 562

NMR struc:

1 models

Authors:

P.Simpson

Key ref:

A.Cehovin et al. (2013). Specific DNA recognition mediated by a type IV pilin. Proc Natl Acad Sci U S A, 110, 3065-3070. PubMed id: 23386723 DOI: 10.1073/pnas.1218832110

Date:

21-Jan-13 Release date: 13-Feb-13

Protein chain

C9X2N5  (C9X2N5_NEIM8) -

DOI no: 10.1073/pnas.1218832110

Proc Natl Acad Sci U S A 110:3065-3070 (2013)

PubMed id: 23386723

Specific DNA recognition mediated by a type IV pilin.

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.

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.