The 8-nm spaghetti: well-structured glycans coating linear tetrapeptide repeats discovered from freshwater with CryoSeek
Wang, T.; Sun, Y.; Li, Z.; Yan, N.
Show abstract
We recently developed a research strategy, termed CryoSeek, to identify uncharacterized bio-entities from natural or endogenous resources using cryo-electron microscopy (cryo-EM). Here we report the discovery of a glycofibril whose primary molecular mass is attributed to a thick glycan shell. The 3.3-[A] resolution cryo-EM reconstruction reveals that the only protein component of the glycofibril, which is approximately 8 nm in diameter, is a linear chain of tetrapeptide repeats. Each tetrapeptide repeat consists of a 3,4-dihydroxyproline (diHyp), a Ser or Thr, and two less conserved residues. Two and one glycan chains are respectively O-linked to the diHyp and Ser/Thr residues. The protein sequence pattern of this glycofibril is similar to that of our recently observed TLP-4, although the glycan chains are different. We rename the previously characterized glycofibril as TLP-4a and designate this one as TLP-4b. Our discoveries reveal the critical role of glycans in structural folding of glycoconjugates and shed light on understanding the carbon/nitrogen ratio in biospheres.
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Interdigitated immunoglobulin arrays form the hyperstable surface layer of the extremophilic bacterium Deinococcus radiodurans 95%
- Cryo-EM structure of the conjugation H-pilus reveals the cyclic nature of the TrhA pilin 94%
- Dynamic structural order of a low complexity domain facilitates assembly of intermediate filaments 94%
Similar papers in this journal
Similar papers in this journal
- Cryo-EM structure of the Agrobacterium tumefaciens T-pilus reveals the importance of positive charges in the lumen 94%
- In situ structure of the AcrAB-TolC efflux pump at subnanometer resolution 93%
- Structural bases for the Charcot-Marie-Tooth disease induced by single amino acid substitutions of myelin protein zero 93%
Similar papers in this journal
- pytom-match-pick: a tophat-transform constraint for automated classification in template matching 92%
- Protein identification using cryo-EM and artificial intelligence guides improved sample purification 92%
- Crystallographic and cryogenic electron microscopic structures and enzymatic characterization of sulfur oxygenase reductase from Sulfurisphaera tokodaii 91%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.