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TitleStructural and mechanistic basis for protein glutamylation by the kinase fold.
Journal, issue, pagesMol Cell, Vol. 81, Issue 21, Page 4527-44539.e8, Year 2021
Publish dateNov 4, 2021
AuthorsAdam Osinski / Miles H Black / Krzysztof Pawłowski / Zhe Chen / Yang Li / Vincent S Tagliabracci /
PubMed AbstractThe kinase domain transfers phosphate from ATP to substrates. However, the Legionella effector SidJ adopts a kinase fold, yet catalyzes calmodulin (CaM)-dependent glutamylation to inactivate the SidE ...The kinase domain transfers phosphate from ATP to substrates. However, the Legionella effector SidJ adopts a kinase fold, yet catalyzes calmodulin (CaM)-dependent glutamylation to inactivate the SidE ubiquitin ligases. The structural and mechanistic basis in which the kinase domain catalyzes protein glutamylation is unknown. Here we present cryo-EM reconstructions of SidJ:CaM:SidE reaction intermediate complexes. We show that the kinase-like active site of SidJ adenylates an active-site Glu in SidE, resulting in the formation of a stable reaction intermediate complex. An insertion in the catalytic loop of the kinase domain positions the donor Glu near the acyl-adenylate for peptide bond formation. Our structural analysis led us to discover that the SidJ paralog SdjA is a glutamylase that differentially regulates the SidE ligases during Legionella infection. Our results uncover the structural and mechanistic basis in which the kinase fold catalyzes non-ribosomal amino acid ligations and reveal an unappreciated level of SidE-family regulation.
External linksMol Cell / PubMed:34407442 / PubMed Central
MethodsEM (single particle)
Resolution2.5 - 2.8 Å
Structure data

23862

7mir

EMDB-23862, PDB-7mir:
Cryo-EM structure of SidJ-SdeA-CaM reaction intermediate complex
Method: EM (single particle) / Resolution: 2.5 Å

23863

7mis

EMDB-23863, PDB-7mis:
Cryo-EM structure of SidJ-SdeC-CaM reaction intermediate complex
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM / Adenosine monophosphate

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-CA:
Unknown entry

ChemComp-NA:
Unknown entry

Source
  • legionella pneumophila (bacteria)
  • homo sapiens (human)
KeywordsTRANSFERASE / HYDROLASE/LIGASE / SidJ / SdeA / CaM / complex / Intermediate / Acyl / Adenylate / Legionella / Ubiquitination / HYDROLASE-LIGASE complex / TRANSFERASE/LIGASE / SdeC / TRANSFERASE-LIGASE complex

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