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A comparative structure/function analysis of two type IV pilin DNA receptors defines a novel mode of DNA-binding
File | Description | Size | Format | |
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Manuscript.pdf | Accepted version | 2.85 MB | Adobe PDF | View/Open |
1-s2.0-S0969212616300375-main.pdf | Published version | 2.8 MB | Adobe PDF | View/Open |
Title: | A comparative structure/function analysis of two type IV pilin DNA receptors defines a novel mode of DNA-binding |
Authors: | Berry, J Xu, Y Ward, PN Lea, SM Matthews, SJ Pelicic, V |
Item Type: | Journal Article |
Abstract: | 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. |
Issue Date: | 7-Jun-2016 |
Date of Acceptance: | 4-Apr-2016 |
URI: | http://hdl.handle.net/10044/1/31125 |
DOI: | 10.1016/j.str.2016.04.001 |
ISSN: | 1878-4186 |
Publisher: | Elsevier (Cell Press) |
Start Page: | 926 |
End Page: | 934 |
Journal / Book Title: | Structure |
Volume: | 24 |
Issue: | 6 |
Copyright Statement: | This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
Sponsor/Funder: | Wellcome Trust Wellcome Trust Biotechnology and Biological Sciences Research Council (BBSRC) |
Funder's Grant Number: | 100280/Z/12/Z WT/104933/z/14/z BB/J016764/1 |
Keywords: | Science & Technology Life Sciences & Biomedicine Biochemistry & Molecular Biology Biophysics Cell Biology NEISSERIA-GONORRHOEAE PROTEIN TRANSFORMATION SEQUENCE SYSTEM IDENTIFICATION COMPETENCE ASSIGNMENT FEATURES PREPILIN Amino Acid Motifs Binding Sites Crystallography, X-Ray DNA, Bacterial Fimbriae Proteins Fimbriae, Bacterial Models, Molecular Neisseria Protein Binding Protein Conformation Protein Folding Fimbriae, Bacterial Neisseria Fimbriae Proteins DNA, Bacterial Crystallography, X-Ray Binding Sites Amino Acid Motifs Protein Conformation Protein Binding Protein Folding Models, Molecular Biophysics 03 Chemical Sciences 06 Biological Sciences 08 Information and Computing Sciences |
Publication Status: | Published |
Online Publication Date: | 2016-05-05 |
Appears in Collections: | Department of Infectious Diseases Faculty of Medicine Faculty of Natural Sciences |