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Structure paper

TitleStructure and biochemical analyses suggest that PrkA/YeaG protein of Thermus thermophilus functions as a putative molecular chaperone.
Journal, issue, pagesJ Biochem, Year 2026
Publish dateJun 15, 2026
AuthorsMasayuki Torii / Ryo Kanno / Akira Mizoguchi / Bruno M Humbel / Kazutoshi Tani / Ryoji Masui /
PubMed AbstractProtein 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 ...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.
External linksJ Biochem / PubMed:42294598
MethodsEM (single particle)
Resolution2.3 - 3.2 Å
Structure data

66911

9xip

EMDB-66911, PDB-9xip:
Structure of dodecameric Apo TpkB from Thermus thermophilus
Method: EM (single particle) / Resolution: 2.3 Å

66912

9xiq

EMDB-66912, PDB-9xiq:
Structure of hexameric TpkB bound to AMP-PNP from Thermus thermophilus
Method: EM (single particle) / Resolution: 2.84 Å

66913

9xir

EMDB-66913, PDB-9xir:
Structure of dodecameric TpkB bound to AMP-PNP from Thermus thermophilus
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • thermus thermophilus hb8 (bacteria)
KeywordsSTRUCTURAL GENOMICS / HYPOTHETICAL PROTEIN / ATP-BINDING / PRK/YEAG FAMILY

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