4A5Q

Crystal structure of the chitinase Chi1 fitted into the 3D structure of the Yersinia entomophaga toxin complex

Summary for 4A5Q

• Entry DOI: 10.2210/pdb4a5q/pdb
• Related: 3AO5
• EMDB information: 1978
• Descriptor: CHI1 (1 entity in total)
• Functional Keywords: hydrolase, bacterial toxin, insecticide
• Biological source: YERSINIA ENTOMOPHAGA
• Total number of polymer chains: 5
• Total formula weight: 303631.78

Authors

Busby, J.N.,Landsberg, M.J.,Simpson, R.M.,Jones, S.A.,Hankamer, B.,Hurst, M.R.H.,Lott, J.S. (deposition date: 2011-10-27, release date: 2011-11-16, Last modification date: 2024-01-31)

Primary citation

Busby, J.N.,Landsberg, M.J.,Simpson, R.M.,Jones, S.A.,Hankamer, B.,Hurst, M.R.H.,Lott, J.S.
Structural Analysis of Chi1 Chitinase from Yen-Tc: The Multisubunit Insecticidal Abc Toxin Complex of Yersinia Entomophaga.
J.Mol.Biol., 415:359-, 2012

PubMed Abstract: Yersinia entomophaga MH96 is a native New Zealand soil bacterium that secretes a large ABC-type protein toxin complex, Yen-Tc, similar to those produced by nematode-associated bacteria such as Photorhabdus luminescens. Y. entomophaga displays an exceptionally virulent pathogenic phenotype in sensitive insect species, causing death within 72 h of infection. Because of this phenotype, there is intrinsic interest in the mechanism of action of Yen-Tc, and it also has the potential to function as a novel class of biopesticide. We have identified genes that encode chitinases as part of the toxin complex loci in Y. entomophaga MH96, P. luminescens, Photorhabdus asymbiotica and Xenorhabdus nematophila. Furthermore, we have shown that the secreted toxin complex from Y. entomophaga MH96 includes two chitinases as an integral part of the complex, a feature not described previously in other ABC toxins and possibly related to the severe disease caused by this bacterium. We present here the structure of the Y. entomophaga MH96 Chi1 chitinase, determined by X-ray crystallography to 1.74 Å resolution, and show that a ring of five symmetrically arranged lobes on the surface of the Yen-Tc toxin complex structure, as determined by single-particle electron microscopy, provides a good fit to the Chi1 monomer. We also confirm that the isolated chitinases display endochitinase activity, as does the complete toxin complex.

PubMed: 22108167
DOI: 10.1016/J.JMB.2011.11.018

Experimental method

ELECTRON MICROSCOPY (17 Å)