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TitleSingle tryptophan Y160W mutant of homooligomeric E. coli purine nucleoside phosphorylase implies that dimers forming the hexamer are functionally not equivalent.
Journal, issue, pagesSci Rep, Vol. 11, Page 11144-11144, Year 2021
Publish dateJan 31, 2020 (structure data deposition date)
AuthorsNarczyk, M. / Mioduszewski, L. / Oksiejuk, A. / Winiewska-Szajewska, M. / Wielgus-Kutrowska, B. / Gojdz, A. / Ciesla, J. / Bzowska, A.
External linksSci Rep / PubMed:34045551
MethodsX-ray diffraction
Resolution1.65000304482 Å
Structure data

PDB-6xz2:
Crystal structure of E. Coli purine nucleoside phosphorylase mutant Y160W with SO4 and Formycin A
Method: X-RAY DIFFRACTION / Resolution: 1.65000304482 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-FMC:
(1S)-1-(7-amino-1H-pyrazolo[4,3-d]pyrimidin-3-yl)-1,4-anhydro-D-ribitol

ChemComp-HOH:
WATER

Source
  • escherichia coli (strain k12) (bacteria)
KeywordsTRANSFERASE / trimer of dimers / single tryptophan mutant / protein-inhibitor complex

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