Imperial College London

Prof Steve Matthews

Faculty of Natural SciencesDepartment of Life Sciences

Professor of Chemical and Structural Biology
 
 
 
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Contact

 

+44 (0)20 7594 5315s.j.matthews Website

 
 
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Location

 

Room 602Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Berry:2016:10.1016/j.str.2016.04.001,
author = {Berry, J-L and Xu, Y and Ward, PN and Lea, SM and Matthews, SJ and Pelicic, V},
doi = {10.1016/j.str.2016.04.001},
journal = {Structure},
pages = {926--934},
title = {A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding.},
url = {http://dx.doi.org/10.1016/j.str.2016.04.001},
volume = {24},
year = {2016}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - DNA transformation is a widespread process allowing bacteria to capture free DNA by using filamentous nano-machines composed of type IV pilins. These proteins can act as DNA receptors as demonstrated by the finding that Neisseria meningitidis ComP minor pilin has intrinsic DNA-binding ability. ComP binds DNA better when it contains the DNA-uptake sequence (DUS) motif abundant in this species genome, playing a role in its trademark ability to selectively take up its own DNA. Here, we report high-resolution structures for meningococcal ComP and Neisseria subflava ComPsub, which recognize different DUS motifs. We show that they are structurally identical type IV pilins that pack readily into filament models and display a unique DD region delimited by two disulfide bonds. Functional analysis of ComPsub defines a new mode of DNA binding involving the DD region, adapted for exported DNA receptors.
AU - Berry,J-L
AU - Xu,Y
AU - Ward,PN
AU - Lea,SM
AU - Matthews,SJ
AU - Pelicic,V
DO - 10.1016/j.str.2016.04.001
EP - 934
PY - 2016///
SP - 926
TI - A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding.
T2 - Structure
UR - http://dx.doi.org/10.1016/j.str.2016.04.001
UR - https://www.ncbi.nlm.nih.gov/pubmed/27161979
UR - http://hdl.handle.net/10044/1/31125
VL - 24
ER -