9xip: Difference between revisions
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==Structure of dodecameric Apo TpkB from Thermus thermophilus== | |||
<StructureSection load='9xip' size='340' side='right'caption='[[9xip]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9xip]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9XIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9XIP 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]] 2.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9xip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9xip OCA], [https://pdbe.org/9xip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9xip RCSB], [https://www.ebi.ac.uk/pdbsum/9xip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9xip ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SK09_THET8 Q5SK09_THET8] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein phosphorylation, a key post-translational modification, is mediated by various protein kinases. The bacterial PrkA/YeaG is recognized as an atypical protein kinase, but its activity remains elusive. This study investigated the structural and functional characteristics of a PrkA/YeaG homologue, TpkB, from Thermus thermophilus HB8. Using cryo-electron microscopy, the structures of TpkB in apo and AMPPNP-bound forms were determined, revealing a hexameric ring architecture characteristic of AAA + superfamily proteins. The TpkB protomer is comprised of an N-terminal domain, an ATPase domain, and a LID domain. The ATPase domain contains conserved sequence motifs associated with ATPase activity, whereas the other domains present a novel fold. TpkB exhibits structural similarity to MoxR family proteins, which possess chaperone-like functions in conjunction with von Willebrand factor A (vWA) domain proteins. Structural and gene neighborhood analyses suggested a functional link between PrkA/YeaG proteins and vWA domain proteins. Biochemical analyses demonstrated that TpkB exhibited ATPase activity and chaperone-like activity, but lacked detectable protein kinase activity. These findings establish TpkB as a novel member of the AAA+ superfamily with potential chaperone functions, providing new insights into the PrkA/YeaG family. | |||
Structure and biochemical analyses suggest that PrkA/YeaG protein of Thermus thermophilus functions as a putative molecular chaperone.,Torii M, Kanno R, Mizoguchi A, Humbel BM, Tani K, Masui R J Biochem. 2026 Jun 15:mvag041. doi: 10.1093/jb/mvag041. PMID:42294598<ref>PMID:42294598</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9xip" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Humbel B]] | |||
[[Category: Kanno R]] | |||
[[Category: Masui R]] | |||
[[Category: Mizoguchi A]] | |||
[[Category: Tani K]] | |||
[[Category: Torri M]] | |||
