1.C.39.4.7
Gram-negative insecticidal protein, GNIP1Aa of 536 aas and 0 TMSs/  Its structure has been determined to 2.5 Å resolution (PDB# 6FBM) (Zaitseva et al. 2019). It consists of two structurally distinct domains, a MACPF domain and a previously uncharacterized type of domain. GNIP1Aa is unique in being a prokaryotic MACPF member to have both its structure and function identified. It is specifically toxic to Diabrotica virgifera virgifera larvae upon feeding. The MACPF domain is probably important for oligomerization and transmembrane pore formation, while the accompanying domain may define the specificity of the target of toxicity. In GNIP1Aa the accompanying C-terminal domain has a unique fold composed of three pseudosymmetric subdomains with shared sequence similarity, a feature not obvious from the initial sequence examination. This domain is in a family named beta-tripod. Important regions in the beta-tripod domain, which may be involved in target recognition, have been identified (Zaitseva et al. 2019).