5kua

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'''Unreleased structure'''
 
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The entry 5kua is ON HOLD until Paper Publication
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==Cryo-EM reconstruction of Neisseria meningitidis Type IV pilus==
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<StructureSection load='5kua' size='340' side='right' caption='[[5kua]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5kua]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KUA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KUA FirstGlance]. <br>
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</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=5kua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kua OCA], [http://pdbe.org/5kua PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kua RCSB], [http://www.ebi.ac.uk/pdbsum/5kua PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kua ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Neisseria meningitidis use Type IV pili (T4P) to adhere to endothelial cells and breach the blood brain barrier, causing cause fatal meningitis. T4P are multifunctional polymers of the major pilin protein, which share a conserved hydrophobic N terminus that is a curved extended alpha-helix, alpha1, in X-ray crystal structures. Here we report a 1.44 A crystal structure of the N. meningitidis major pilin PilE and a approximately 6 A cryo-electron microscopy reconstruction of the intact pilus, from which we built an atomic model for the filament. This structure reveals the molecular arrangement of the N-terminal alpha-helices in the filament core, including a melted central portion of alpha1 and a bridge of electron density consistent with a predicted salt bridge necessary for pilus assembly. This structure has important implications for understanding pilus biology.
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Authors: Kolappan, S., Coureuil, M., Yu, X., Nassif, X., Craig, L., Egelman, E.H.
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Structure of the Neisseria meningitidis Type IV pilus.,Kolappan S, Coureuil M, Yu X, Nassif X, Egelman EH, Craig L Nat Commun. 2016 Oct 4;7:13015. doi: 10.1038/ncomms13015. PMID:27698424<ref>PMID:27698424</ref>
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Description: Cryo-EM reconstruction of Neisseria meningitidis Type IV pilus
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5kua" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Neisseria meningitidis]]
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[[Category: Coureuil, M]]
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[[Category: Craig, L]]
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[[Category: Egelman, E H]]
[[Category: Kolappan, S]]
[[Category: Kolappan, S]]
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[[Category: Egelman, E.H]]
 
[[Category: Nassif, X]]
[[Category: Nassif, X]]
[[Category: Yu, X]]
[[Category: Yu, X]]
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[[Category: Coureuil, M]]
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[[Category: Melted helix]]
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[[Category: Craig, L]]
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[[Category: Protein fibril]]
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[[Category: Type iv pili]]

Revision as of 09:23, 19 October 2016

Cryo-EM reconstruction of Neisseria meningitidis Type IV pilus

5kua, resolution 6.00Å

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