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A comparative structure/function analysis of two type IV pilin DNA receptors defines a novel mode of DNA-binding

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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