ZNG1B
Function
Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1B to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1.
Sequence Similarities
Belongs to the SIMIBI class G3E GTPase family. ZNG1 subfamily.
Cellular localization
- Nucleus
Alternative names
CBWD2, ZNG1B, Zinc-regulated GTPase metalloprotein activator 1B, Cobalamin synthase W domain-containing protein 2, COBW domain-containing protein 2