Nordling, Kerstin
- Karolinska institutet
Sammanfattning
Conversion of spider silk proteins from soluble dope to insoluble fibers involves pH-dependent dimerization of the N-terminal domain (NT). This conversion is tightly regulated to prevent premature precipitation and enable rapid silk formation at the end of the duct. Three glutamic acid residues that mediate this process in the NT from Euprosthenops australis major ampullate spidroin 1 are well conserved among spidroins. However, NTs of minor ampullate spidroins from several species, including Araneus ventricosus ((Av)MiSp NT), lack one of the glutamic acids. Here we investigate the pH-dependent structural changes of (Av)MiSp NT, revealing that it uses the same mechanism but involves a non-conserved glutamic acid residue instead. Homology modeling of the structures of other MiSp NTs suggests that these harbor different compensatory residues. This indicates that, despite sequence variations, the molecular mechanism underlying pH-dependent dimerization of NT is conserved among different silk types.
Nyckelord
NMR structure; pH sensitivity; protein conformation; spidroins
Publicerad i
ChemBioChem
2015, volym: 16, nummer: 12, sidor: 1720-1724
Utgivare: WILEY-V C H VERLAG GMBH
SLU författare
Rising, Anna
- Institutionen för husdjurens biovetenskaper, Sveriges lantbruksuniversitet
- Karolinska institutet
- Institutionen för husdjurens biovetenskaper, Sveriges lantbruksuniversitet
Johansson, Jan
- Institutionen för husdjurens biovetenskaper, Sveriges lantbruksuniversitet
- Karolinska institutet
- Tallinna Ülikool
- Institutionen för husdjurens biovetenskaper, Sveriges lantbruksuniversitet
UKÄ forskningsämne
Cell- och molekylärbiologi
Publikationens identifierare
- DOI: https://doi.org/10.1002/cbic.201500263
Permanent länk till denna sida (URI)
https://res.slu.se/id/publ/68644