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Structure paper

TitleStructural mechanisms of allosteric regulation in the human cis-prenyltransferase complex.
Journal, issue, pagesNat Commun, Vol. 16, Page 10786-10786, Year 2025
Publish dateApr 24, 2025 (structure data deposition date)
AuthorsGiladi, M. / Kredi, S. / Guardiani, C. / Aviram, L. / Vankova, P. / Gaizinger, Y. / Man, P. / Giacomello, A. / Haitin, Y.
External linksNat Commun / PubMed:41315348
MethodsX-ray diffraction
Resolution2.4 - 2.89 Å
Structure data

PDB-9r08:
Structure of the human heterotetrameric cis-prenyltransferase complex harboring NgBR-S249A in complex with magnesium, FsPP and IPP
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-9r0e:
Structure of the human heterotetrameric cis-prenyltransferase complex harboring NgBR-S249T in complex with magnesium, FsPP and IPP
Method: X-RAY DIFFRACTION / Resolution: 2.82 Å

PDB-9r0k:
Structure of the human heterotetrameric cis-prenyltransferase complex in its apo form
Method: X-RAY DIFFRACTION / Resolution: 2.89 Å

Chemicals

ChemComp-IPE:
3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE

ChemComp-FPS:
S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL] TRIHYDROGEN THIODIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GLY:
GLYCINE

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / cis-prenyltransferase / dolichol

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