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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 dateNov 3, 2025 (structure data deposition date)
AuthorsTorii, M. / Kanno, R. / Mizoguchi, A. / Humbel, B.M. / Tani, K. / Masui, R.
External linksJ. Biochem. / PubMed:42294598
MethodsEM (single particle)
Resolution2.3 - 3.2 Å
Structure data

PDB-9xip:
Structure of dodecameric Apo TpkB from Thermus thermophilus
Method: ELECTRON MICROSCOPY / Resolution: 2.3 Å

PDB-9xiq:
Structure of hexameric TpkB bound to AMP-PNP from Thermus thermophilus
Method: ELECTRON MICROSCOPY / Resolution: 2.84 Å

PDB-9xir:
Structure of dodecameric TpkB bound to AMP-PNP from Thermus thermophilus
Method: ELECTRON MICROSCOPY / 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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