Structure-function characterization of an insecticidal protein GNIP1Aa, a member of an MACPF and β-tripod families
| Autor: | Christian Krebs, James R. Doroghazi, Sara L. Milam, Deepa Balasubramanian, Joerg Freigang, Jelena Zaitseva, Daniel Vaknin, Nicholas B. Duck |
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| Rok vydání: | 2019 |
| Předmět: |
Models
Molecular Pore Forming Cytotoxic Proteins Insecticides Protein family Computational biology Complement Membrane Attack Complex Crystallography X-Ray Bacterial Proteins Protein Domains Protein oligomerization Animals Amino Acid Sequence MACPF Multidisciplinary biology Chemistry Perforin Chromobacterium Structure function Initial sequence Transmembrane protein Protein Structure Tertiary Coleoptera PNAS Plus biology.protein Complement membrane attack complex |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 116(8) |
| ISSN: | 1091-6490 |
| Popis: | 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 Chromobacterium piscinae strain and is specifically toxic to Diabrotica virgifera virgifera 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. |
| Databáze: | OpenAIRE |
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