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TitleStructural and functional analysis of LarC, a CTP-dependent cyclometallase required for nickel-pincer nucleotide cofactor biosynthesis.
Journal, issue, pagesSci Adv, Vol. 12, Issue 35, Page eaeh6867, Year 2026
Publish dateAug 28, 2026
AuthorsRobert Wolfe / Aiko Turmo / Samantha Velasquez-Rivertte / Dexin Sui / Diego Granados-Villanueva / Benoit Desguin / Jian Hu / Robert P Hausinger / Kelly H Kim /
PubMed AbstractBiosynthesis of the nickel-pincer mononucleotide metallocofactor requires a CTP-dependent nickel insertion reaction catalyzed by LarC, whose mechanism of C-Ni bond formation is not fully understood. ...Biosynthesis of the nickel-pincer mononucleotide metallocofactor requires a CTP-dependent nickel insertion reaction catalyzed by LarC, whose mechanism of C-Ni bond formation is not fully understood. Here, we report the first cryo-electron microscopy structures of full-length LarC from with and without a mimic of the CMPylated reaction intermediate. LarC assembles as a hexamer comprising a central LarC2 domain core and peripheral LarC1 domain trimers connected by long, flexible interdomain linkers. The LarC1 domains contain a conserved histidine-rich region for nickel binding and an adjacent conserved acidic pocket, both essential for activity. Structural modeling suggests that the intermediate binds within the acidic pocket adjacent to the putative nickel-binding site, while cryo-EM density for an intermediate analog identifies an interdomain cleft near the LarC2 CTP-binding site as a likely transfer site. Based on these findings, we propose that the intermediate is transferred through the interdomain cleft from LarC2, where it is CMPylated, to LarC1 for nickel insertion.
External linksSci Adv / PubMed:42647608 / PubMed Central
MethodsEM (single particle)
Resolution3.33 - 3.97 Å
Structure data

76279

12bi

EMDB-76279, PDB-12bi:
Moorella thermoacetica LarC (conformation 1)
Method: EM (single particle) / Resolution: 3.97 Å

76280

12bj

EMDB-76280, PDB-12bj:
Moorella thermoacetica LarC (conformation 2)
Method: EM (single particle) / Resolution: 3.85 Å

76281

12bk

EMDB-76281, PDB-12bk:
Moorella thermoacetica LarC (conformation 3)
Method: EM (single particle) / Resolution: 3.87 Å

76282

12bl

EMDB-76282, PDB-12bl:
Moorella thermoacetica LarC in complex with P2TAD
Method: EM (single particle) / Resolution: 3.33 Å

Chemicals

PDB-1dch:
CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR

Source
  • Neomoorella thermoacetica (bacteria)
  • moorella thermoacetica (strain atcc 39073 / jcm 9320) (bacteria)
KeywordsMETAL BINDING PROTEIN / Enzyme / Nickel insertase / Cyclometalliase

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