3j1r

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[[Image:3j1r.png|left|200px]]
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==Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices==
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<StructureSection load='3j1r' size='340' side='right' caption='[[3j1r]], [[Resolution|resolution]] 7.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3j1r]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Ignicoccus_hospitalis Ignicoccus hospitalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J1R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J1R FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j1r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j1r RCSB], [http://www.ebi.ac.uk/pdbsum/3j1r PDBsum]</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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Bacterial motility is driven by the rotation of flagellar filaments that supercoil. The supercoiling involves the switching of coiled-coil protofilaments between two different states. In archaea, the flagellar filaments responsible for motility are formed by proteins with distinct homology in their N-terminal portion to bacterial Type IV pilins. The bacterial pilins have a single N-terminal hydrophobic alpha-helix, not the coiled coil found in flagellin. We have used electron cryo-microscopy to study the adhesion filaments from the archaeon Ignicoccus hospitalis. While I. hospitalis is non-motile, these filaments make transitions between rigid stretches and curved regions and appear morphologically similar to true archaeal flagellar filaments. A resolution of ~7.5A allows us to unambiguously build a model for the packing of these N-terminal alpha-helices, and this packing is different from several bacterial Type IV pili whose structure has been analyzed by electron microscopy and modeling. Our results show that the mechanism responsible for the supercoiling of bacterial flagellar filaments cannot apply to archaeal filaments.
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{{STRUCTURE_3j1r| PDB=3j1r | SCENE= }}
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Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-Terminal Type IV Pilin Helices.,Yu X, Goforth C, Meyer C, Rachel R, Wirth R, Schroder GF, Egelman EH J Mol Biol. 2012 May 30. PMID:22659006<ref>PMID:22659006</ref>
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===Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_22659006}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[3j1r]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Ignicoccus_hospitalis Ignicoccus hospitalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J1R OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:022659006</ref><references group="xtra"/>
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[[Category: Ignicoccus hospitalis]]
[[Category: Ignicoccus hospitalis]]
[[Category: Egelman, E H.]]
[[Category: Egelman, E H.]]

Revision as of 06:59, 9 June 2014

Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices

3j1r, resolution 7.50Å

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