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3jc8

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<SX load='3jc8' size='340' side='right' viewer='molstar' caption='[[3jc8]]' scene=''>
<SX load='3jc8' size='340' side='right' viewer='molstar' caption='[[3jc8]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3jc8]] is a 115 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus_dk_1622 Myxococcus xanthus dk 1622]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JC8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3jc8]] is a 115 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus_DK_1622 Myxococcus xanthus DK 1622]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JC8 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MEA:N-METHYLPHENYLALANINE'>MEA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3jc9|3jc9]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MEA:N-METHYLPHENYLALANINE'>MEA</scene></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=3jc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jc8 OCA], [https://pdbe.org/3jc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jc8 RCSB], [https://www.ebi.ac.uk/pdbsum/3jc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jc8 ProSAT]</span></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=3jc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jc8 OCA], [https://pdbe.org/3jc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jc8 RCSB], [https://www.ebi.ac.uk/pdbsum/3jc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jc8 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/PILB_MYXXD PILB_MYXXD] ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers. Acts as a molecular motor to provide the energy that is required for biogenesis of the pilus and the extrusion of substrates generated in the cytoplasm (PubMed:28779124, PubMed:26965631). PilB ATPase activity is also essential for T4P extension while antagonist PilT ATPase activity is required for T4P retraction (PubMed:18223089). In addition, functions as a regulator of exopolysaccharide (EPS) downstream of the T4P filament and upstream of the Dif signaling (PubMed:28779124).<ref>PMID:18223089</ref> <ref>PMID:26965631</ref> <ref>PMID:28779124</ref>
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Type IVa pili are filamentous cell surface structures observed in many bacteria. They pull cells forward by extending, adhering to surfaces, and then retracting. We used cryo-electron tomography of intact Myxococcus xanthus cells to visualize type IVa pili and the protein machine that assembles and retracts them (the type IVa pilus machine, or T4PM) in situ, in both the piliated and nonpiliated states, at a resolution of 3 to 4 nanometers. We found that T4PM comprises an outer membrane pore, four interconnected ring structures in the periplasm and cytoplasm, a cytoplasmic disc and dome, and a periplasmic stem. By systematically imaging mutants lacking defined T4PM proteins or with individual proteins fused to tags, we mapped the locations of all 10 T4PM core components and the minor pilins, thereby providing insights into pilus assembly, structure, and function.
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Architecture of the type IVa pilus machine.,Chang YW, Rettberg LA, Treuner-Lange A, Iwasa J, Sogaard-Andersen L, Jensen GJ Science. 2016 Mar 11;351(6278):aad2001. doi: 10.1126/science.aad2001. Epub 2016, Mar 10. PMID:26965631<ref>PMID:26965631</ref>
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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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<div class="pdbe-citations 3jc8" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myxococcus xanthus dk 1622]]
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[[Category: Myxococcus xanthus DK 1622]]
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[[Category: Chang, Y W]]
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[[Category: Chang Y-W]]
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[[Category: Jensen, G J]]
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[[Category: Jensen GJ]]
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[[Category: Rettberg, L A]]
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[[Category: Rettberg LA]]
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[[Category: Membrane channel]]
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[[Category: Motor]]
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[[Category: Motor protein]]
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[[Category: Pilus]]
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[[Category: Ring]]
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Revision as of 08:43, 7 February 2024

Architectural model of the type IVa pilus machine in a piliated state

3jc8

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