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A family of papain-like fungal chimerolectins with distinct Ca2+-dependent activation mechanism

Cordara, Gabriele; Manna, Dipankar; Krengel, Ute
Journal article; AcceptedVersion; Peer reviewed
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Cordara_Biochemistry+2017_accepted+manuscript.pdf (2.873Mb)
Year
2017
Permanent link
http://urn.nb.no/URN:NBN:no-71667

CRIStin
1481533

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  • Kjemisk institutt [843]
  • CRIStin høstingsarkiv [15923]
Original version
Biochemistry. 2017, 56 (35), 4689-4700, DOI: http://dx.doi.org/10.1021/acs.biochem.7b00317
Abstract
An important function of fungal lectins is to protect their host. Marasmius oreades agglutinin (MOA) is toxic to nematodes and exerts its protective effect through protease activity. Its proteolytic function is associated with a papain-like dimerization domain. The closest homologue of MOA is Polyporus squamosus lectin 1a (PSL1a). Here, we probed PSL1a for catalytic activity and confirmed that it is a calcium-dependent cysteine protease, like MOA. The X-ray crystal structures of PSL1a (1.5 Å) and MOA (1.3 Å) in complex with calcium and the irreversible cysteine protease inhibitor E-64 elucidated the structural basis for their mechanism of action. The comparison with other calcium-dependent proteases (calpains, LapG) reveals a unique metal-dependent activation mechanism relying on a calcium-induced backbone shift and intradimer cooperation. Intriguingly, the enzymes appear to use a tyrosine-gating mechanism instead of pro-peptide processing. A search for potential MOA orthologues suggests the existence of a whole new family of fungal chimerolectins with these unique features.
 
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