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Structure paper

TitleSpecificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD.
Journal, issue, pagesNat Commun, Vol. 12, Page 2426-2426, Year 2021
Publish dateJul 2, 2020 (structure data deposition date)
AuthorsFauser, J. / Gulen, B. / Pogenberg, V. / Pett, C. / Pourjafar-Dehkordi, D. / Krisp, C. / Hopfner, D. / Konig, G. / Schluter, H. / Feige, M.J. ...Fauser, J. / Gulen, B. / Pogenberg, V. / Pett, C. / Pourjafar-Dehkordi, D. / Krisp, C. / Hopfner, D. / Konig, G. / Schluter, H. / Feige, M.J. / Zacharias, M. / Hedberg, C. / Itzen, A.
External linksNat Commun / PubMed:33893288
MethodsX-ray diffraction
Resolution2.64 Å
Structure data

PDB-6zmd:
Crystal structure of HYPE covalently tethered to BiP bound to AMP-PNP
Method: X-RAY DIFFRACTION / Resolution: 2.64 Å

Chemicals

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

ChemComp-QMK:
~{N}-[2-[1-[(2~{R},3~{R},4~{S},5~{R})-3,4-bis(oxidanyl)-5-[[tris(oxidanyl)-$l^{5}-phosphanyl]oxymethyl]oxolan-2-yl]-1,2,3-triazol-4-yl]ethyl]ethanamide

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / AMPylation / Endoplasmic reticulum / Fic enzyme / chaperone / post-translational modification

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