5V3S

Crystal structure of IP-1A from Alcaligenes faecalis at 1.8A resolution

Summary for 5V3S

• Entry DOI: 10.2210/pdb5v3s/pdb
• Descriptor: Two-component insecticidal protein 16 kDa unit (2 entities in total)
• Functional Keywords: insecticidal toxin, aegerolysin, toxin
• Biological source: Alcaligenes faecalis
• Total number of polymer chains: 2
• Total formula weight: 34751.68

Authors

Yalpani, N.,Altier, D.,Guan, R.,Montelione, G. (deposition date: 2017-03-08, release date: 2017-06-14, Last modification date: 2024-10-23)

Primary citation

Yalpani, N.,Altier, D.,Barry, J.,Kassa, A.,Nowatzki, T.M.,Sethi, A.,Zhao, J.Z.,Diehn, S.,Crane, V.,Sandahl, G.,Guan, R.,Poland, B.,Perez Ortega, C.,Nelson, M.E.,Xie, W.,Liu, L.,Wu, G.
An Alcaligenes strain emulates Bacillus thuringiensis producing a binary protein that kills corn rootworm through a mechanism similar to Cry34Ab1/Cry35Ab1.
Sci Rep, 7:3063-3063, 2017

PubMed Abstract: Crops expressing Bacillus thuringiensis (Bt)-derived insecticidal protein genes have been commercially available for over 15 years and are providing significant value to growers. However, there remains the need for alternative insecticidal actives due to emerging insect resistance to certain Bt proteins. A screen of bacterial strains led to the discovery of a two-component insecticidal protein named AfIP-1A/1B from an Alcaligenes faecalis strain. This protein shows selectivity against coleopteran insects including western corn rootworm (WCR). Transgenic maize plants expressing AfIP-1A/1B demonstrate strong protection from rootworm injury. Surprisingly, although little sequence similarity exists to known insecticidal proteins, efficacy tests using WCR populations resistant to two different Cry proteins show that AfIP-1A/1B and mCry3A differ in their mode of action while AfIP-1A/1B and the binary Cry34Ab1/Cry35Ab1 protein share a similar mode. These findings are supported by results of competitive binding assays and the similarity of the x-ray structure of AfIP-1A to Cry34Ab1. Our work indicates that insecticidal proteins obtained from a non-Bt bacterial source can be useful for developing genetically modified crops and can function similarly to familiar proteins from Bt.

PubMed: 28596570
DOI: 10.1038/s41598-017-03544-9

Experimental method

X-RAY DIFFRACTION (1.8 Å)