2nba
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Solution NMR structure of the minor DNA-uptake pilin ComP from Neisseri subflava== | |
+ | <StructureSection load='2nba' size='340' side='right' caption='[[2nba]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2nba]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NBA FirstGlance]. <br> | ||
+ | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hz7|5hz7]]</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nba OCA], [http://pdbe.org/2nba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nba RCSB], [http://www.ebi.ac.uk/pdbsum/2nba PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding.,Berry JL, Xu Y, Ward PN, Lea SM, Matthews SJ, Pelicic V Structure. 2016 May 3. pii: S0969-2126(16)30037-5. doi:, 10.1016/j.str.2016.04.001. PMID:27161979<ref>PMID:27161979</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 2nba" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Berry, J L]] | ||
[[Category: Xu, Y]] | [[Category: Xu, Y]] | ||
- | [[Category: | + | [[Category: Dna binding protein]] |
+ | [[Category: Dna transformation]] | ||
+ | [[Category: Dna-binding]] | ||
+ | [[Category: Neisseriaceae]] | ||
+ | [[Category: Type iv pilin]] |
Revision as of 07:41, 1 June 2016
Solution NMR structure of the minor DNA-uptake pilin ComP from Neisseri subflava
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