View source for 10mz


==Single particle reconstruction of PilU from Vibrio cholerae El Tor E7946, form 2==
<StructureSection load='10mz' size='340' side='right'caption='[[10mz]], [[Resolution|resolution]] 3.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[10mz]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=10MZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=10MZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.68&#8491;</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=10mz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=10mz OCA], [https://pdbe.org/10mz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=10mz RCSB], [https://www.ebi.ac.uk/pdbsum/10mz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=10mz ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Type IV pili (T4P) mediate surface motility, host interactions, and DNA uptake through cycles of extension and retraction. While the primary retraction ATPase PilT has been extensively characterized, its homolog PilU remains less well understood despite being demonstrated as a PilT-dependent retraction ATPase. Here, we determined six PilU structures by cryo-electron microscopy and x-ray crystallography. The structures reveal a homohexameric assembly stabilized by interactions between the C-terminal catalytic domain of one subunit and the N-terminal PAS-like domain of a neighboring subunit. PilU adopts multiple conformational states, exhibiting different combinations of open and closed interfaces even in the absence of nucleotide. Comparison with PilT highlights structural features that likely underlie PilU's weak ATPase activity and its dependence on PilT for function. Together, these findings provide a structural framework for understanding PilU's role within the T4P retraction machinery.

Analysis of the heterogenous structural states of the hexameric ATPase PilU of the type IV pili from Vibrio cholerae.,Guo Y, Shukla S, Minasov G, Inniss NL, Klose T, Tokars VL, Mondragon A, Otwinowski Z, Borek D, Satchell KJF Protein Sci. 2026 Jun;35(6):e70609. doi: 10.1002/pro.70609. PMID:42084485<ref>PMID:42084485</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 10mz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Borek D]]
[[Category: Guo Y]]
[[Category: Klose T]]
[[Category: Mondragon A]]
[[Category: Satchell K]]
[[Category: Shukla S]]
[[Category: Tokars V]]