Structural highlights
FunctionNIF3L_HUMAN May function as a transcriptional corepressor through its interaction with COPS2, negatively regulating the expression of genes involved in neuronal differentiation.[UniProtKB:Q9EQ80] Publication Abstract from PubMedNIF3L1 (also NIF3) is a highly conserved protein belonging to the DUF34 protein family with unknown molecular function, present in bacteria, archaea, and eukaryotes. Here, we present the first crystal structures of human NIF3, revealing a hexameric toroidal assembly with a central cavity gated by PII-like insertion domains. Each subunit contains a mononuclear zinc-binding site, marking a clear departure from the dinuclear metal centers of bacterial homologs and potential functional divergence of the scaffold. We further capture a half-capped state with asymmetric disorder of the insertion domains and local rearrangements near the metal site, suggesting a gating mechanism that regulates access to the internal chamber. These findings uncover an unexpected level of structural plasticity in human NIF3 and provide a framework for future studies investigating whether the different lid conformations observed in our structures have functional relevance in vivo. Crystal structure of human NIF3-like protein reveals dynamic hexameric assembly with a single divalent metal binding site.,Wator-Wilk E, Zak K, Wilk P, Kochanowski P, Maslanka A, Skalniak L, Grudnik P FEBS J. 2026 Sep 15. doi: 10.1111/febs.70724. PMID:42741873[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 16:17, 25 September 2026.