5hz7
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==High-resolution crystal structure of the minor DNA-binding pilin ComP from Neisseria meningitidis in fusion with MBP== | |
| + | <StructureSection load='5hz7' size='340' side='right' caption='[[5hz7]], [[Resolution|resolution]] 1.43Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5hz7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HZ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HZ7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MLR:MALTOTRIOSE'>MLR</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5hz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hz7 OCA], [http://pdbe.org/5hz7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hz7 RCSB], [http://www.ebi.ac.uk/pdbsum/5hz7 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> |
| - | [[Category: | + | <div class="pdbe-citations 5hz7" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Berry, J L]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: Dna transformation]] | ||
| + | [[Category: Dna-binding]] | ||
| + | [[Category: Neisseriaceae]] | ||
| + | [[Category: Type iv pilin]] | ||
Revision as of 08:01, 1 June 2016
High-resolution crystal structure of the minor DNA-binding pilin ComP from Neisseria meningitidis in fusion with MBP
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