6FBM

Crystal structure of GNIP1Aa from Chromobacterium piscinae

Summary for 6FBM

• Entry DOI: 10.2210/pdb6fbm/pdb
• Descriptor: Gram-negative insecticidal protein (2 entities in total)
• Functional Keywords: macpf, toxin
• Biological source: Chromobacterium piscinae
• Total number of polymer chains: 4
• Total formula weight: 235976.84

Authors

Freigang, J.,Zaitseva, J. (deposition date: 2017-12-19, release date: 2019-01-30, Last modification date: 2024-05-08)

Primary citation

Zaitseva, J.,Vaknin, D.,Krebs, C.,Doroghazi, J.,Milam, S.L.,Balasubramanian, D.,Duck, N.B.,Freigang, J.
Structure-function characterization of an insecticidal protein GNIP1Aa, a member of an MACPF and beta-tripod families.
Proc.Natl.Acad.Sci.USA, 116:2897-2906, 2019

PubMed Abstract: The crystal structure of the Gram-negative insecticidal protein, GNIP1Aa, has been solved at 2.5-Å resolution. The protein consists of two structurally distinct domains, a MACPF (membrane attack complex/PerForin) 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 was isolated from a strain and is specifically toxic to larvae upon feeding. In members of the MACPF family, the MACPF domain has been shown to be important for protein oligomerization and formation of transmembrane pores, while accompanying domains define the specificity of the target of the 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. Our analysis places this domain into a protein family, named here β-tripod. Using mutagenesis, we identified functionally important regions in the β-tripod domain, which may be involved in target recognition.

PubMed: 30728296
DOI: 10.1073/pnas.1815547116

Experimental method

X-RAY DIFFRACTION (2.5 Å)