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[[Image:2m3k.png|left|200px]]


{{STRUCTURE_2m3k| PDB=2m3k |  SCENE= }}
==Global fold of the type IV pilin ComP from Neisseria meningitidis==
<StructureSection load='2m3k' size='340' side='right'caption='[[2m3k]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2m3k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M3K FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m3k OCA], [https://pdbe.org/2m3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m3k RCSB], [https://www.ebi.ac.uk/pdbsum/2m3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m3k ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===Global fold of the type IV pilin ComP from Neisseria meningitidis===
Specific DNA recognition mediated by a type IV pilin.,Cehovin A, Simpson PJ, McDowell MA, Brown DR, Noschese R, Pallett M, Brady J, Baldwin GS, Lea SM, Matthews SJ, Pelicic V Proc Natl Acad Sci U S A. 2013 Feb 5. PMID:23386723<ref>PMID:23386723</ref>


{{ABSTRACT_PUBMED_23386723}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m3k" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
[[2m3k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M3K OCA].
*[[Pilin 3D structures|Pilin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria meningitidis]]
[[Category: Neisseria meningitidis]]
[[Category: Simpson, P.]]
[[Category: Simpson P]]
[[Category: Dna uptake]]
[[Category: Motor protein]]

Latest revision as of 08:20, 17 October 2024

Global fold of the type IV pilin ComP from Neisseria meningitidisGlobal fold of the type IV pilin ComP from Neisseria meningitidis

Structural highlights

2m3k is a 1 chain structure with sequence from Neisseria meningitidis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 1 model
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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.

Specific DNA recognition mediated by a type IV pilin.,Cehovin A, Simpson PJ, McDowell MA, Brown DR, Noschese R, Pallett M, Brady J, Baldwin GS, Lea SM, Matthews SJ, Pelicic V Proc Natl Acad Sci U S A. 2013 Feb 5. PMID:23386723[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Cehovin A, Simpson PJ, McDowell MA, Brown DR, Noschese R, Pallett M, Brady J, Baldwin GS, Lea SM, Matthews SJ, Pelicic V. Specific DNA recognition mediated by a type IV pilin. Proc Natl Acad Sci U S A. 2013 Feb 5. PMID:23386723 doi:http://dx.doi.org/10.1073/pnas.1218832110
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