Crystal structure of blue laccase BP76, a unique termite suicidal defense weapon
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články
PubMed
39151418
DOI
10.1016/j.str.2024.07.015
PII: S0969-2126(24)00278-8
Knihovny.cz E-zdroje
- Klíčová slova
- Neocapritermes taracua, X-ray crystallography, autothysis, benzoquinone, colony defence, insect glycosylation, laccase, protein stabilization, single-wavelength anomalous diffraction,
- MeSH
- glykosylace MeSH
- hmyzí proteiny chemie metabolismus MeSH
- Isoptera * MeSH
- katalytická doména MeSH
- krystalografie rentgenová MeSH
- lakasa * chemie metabolismus MeSH
- molekulární modely * MeSH
- multimerizace proteinu MeSH
- sbalování proteinů MeSH
- sekvence aminokyselin MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- hmyzí proteiny MeSH
- lakasa * MeSH
Aging workers of the termite Neocapritermes taracua can defend their colony by sacrificing themselves by body rupture, mixing the externally stored blue laccase BP76 with hydroquinones to produce a sticky liquid rich in toxic benzoquinones. Here, we describe the crystal structure of BP76 isolated from N. taracua in its native form. The structure reveals several stabilization strategies, including compact folding, glycosylation, and flexible loops with disulfide bridges and tight dimer interface. The remarkable stability of BP76 maintains its catalytic activity in solid state during the lifespan of N. taracua workers, providing old workers with an efficient defensive weapon to protect their colony.
Institute of Microbiology Czech Academy of Sciences 142 20 Prague Czech Republic
Okinawa Institute of Science and Technology Graduate University Okinawa 904 0495 Japan
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