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5WV9

Crystal structure of a insect group III chitinase complex with (GlcNAc)6 (CAD1-(GlcNAc)6 ) from Ostrinia furnacalis

Summary for 5WV9
Entry DOI10.2210/pdb5wv9/pdb
Related5WV8 5WVB 5WVF 5WVG 5WVH
Related PRD IDPRD_900017
DescriptorChitinase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
Functional Keywordsostrinia furnacalis, chitinase, three-dimensional structure, chitin metabolism, hydrolase, (glcnac)6
Biological sourceOstrinia furnacalis (Asian corn borer)
Total number of polymer chains1
Total formula weight55297.51
Authors
Liu, T.,Zhou, Y.,Yang, Q. (deposition date: 2016-12-23, release date: 2017-12-27, Last modification date: 2024-11-06)
Primary citationLiu, T.,Zhu, W.,Wang, J.,Zhou, Y.,Duan, Y.,Qu, M.,Yang, Q.
The deduced role of a chitinase containing two nonsynergistic catalytic domains
Acta Crystallogr D Struct Biol, 74:30-40, 2018
Cited by
PubMed Abstract: The glycoside hydrolase family 18 chitinases degrade or alter chitin. Multiple catalytic domains in a glycoside hydrolase family 18 chitinase function synergistically during chitin degradation. Here, an insect group III chitinase from the agricultural pest Ostrinia furnacalis (OfChtIII) is revealed to be an arthropod-conserved chitinase that contains two nonsynergistic GH18 domains according to its catalytic properties. Both GH18 domains are active towards single-chained chitin substrates, but are inactive towards insoluble chitin substrates. The crystal structures of each unbound GH18 domain, as well as of GH18 domains complexed with hexa-N-acetyl-chitohexaose or penta-N-acetyl-chitopentaose, suggest that the two GH18 domains possess endo-specific activities. Physiological data indicated that the developmental stage-dependent gene-expression pattern of OfChtIII was the same as that of the chitin synthase OfChsA but significantly different from that of the chitinase OfChtI, which is indispensable for cuticular chitin degradation. Additionally, immunological staining indicated that OfChtIII was co-localized with OfChsA. Thus, OfChtIII is most likely to be involved in the chitin-synthesis pathway.
PubMed: 29372897
DOI: 10.1107/S2059798317018289
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.105 Å)
Structure validation

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