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Structure paper

TitleCrystal structure, enzymatic and thermodynamic properties of the Thermus thermophilus phage Tt72 lytic endopeptidase with unique structural signatures of thermal adaptation.
Journal, issue, pagesJ. Struct. Biol., Vol. 217, Page 108230-108230, Year 2025
Publish dateFeb 20, 2024 (structure data deposition date)
AuthorsDorawa, S. / Biniek-Antosiak, K. / Bejger, M. / Kaczorowska, A.K. / Ciuchcinski, K. / Godlewska, A. / Plotka, M. / Hreggvidsson, G.O. / Dziewit, L. / Kaczorowski, T. / Rypniewski, W.
External linksJ. Struct. Biol. / PubMed:40580998
MethodsX-ray diffraction
Resolution2.198 - 2.394 Å
Structure data

PDB-8s3m:
LysTt72, a lytic endopeptidase from Thermus thermophilus MAT72 phage vB_Tt72
Method: X-RAY DIFFRACTION / Resolution: 2.198 Å

PDB-8s3u:
LysTt72, a lytic endopeptidase from Thermus thermophilus MAT72 phage vB_Tt72
Method: X-RAY DIFFRACTION / Resolution: 2.301 Å

PDB-8s3w:
LysTt72, a lytic endopeptidase from Thermus thermophilus MAT72 phage vB_Tt72
Method: X-RAY DIFFRACTION / Resolution: 2.394 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • thermus phage tt72 (virus)
  • escherichia coli bl21(de3) (bacteria)
KeywordsVIRAL PROTEIN / Endopeptidase / Metalloprotein / Thermostability / Bacteriophage

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