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TitleCryoSeek II: Cryo-EM analysis of glycofibrils from freshwater reveals well-structured glycans coating linear tetrapeptide repeats.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 1, Page e2423943122, Year 2025
Publish dateJan 7, 2025
AuthorsTongtong Wang / Wenze Huang / Kui Xu / Yitong Sun / Qiangfeng Cliff Zhang / Chuangye Yan / Zhangqiang Li / Nieng Yan /
PubMed AbstractDespite the recent breakthrough in structure determination and prediction of proteins, the structural investigation of carbohydrates remains a challenge. Here, we report the cryo-EM analysis of a ...Despite the recent breakthrough in structure determination and prediction of proteins, the structural investigation of carbohydrates remains a challenge. Here, we report the cryo-EM analysis of a glycofibril found in the freshwater in the Tsinghua Lotus Pond. The fibril, which we name TLP-4, is made of a linear chain of tetrapeptide repeats coated with >4 nm thick glycans. In each repeat, two glycans are O-linked to a 3,4-dihydroxyproline and another glycan attaches to the adjacent Ser or Thr. The fibril structure is entirely maintained through glycan packing. Bioinformatic analysis confirms the conservation of the TLP-4 repeats across species, suggesting the existence of a large number of glycofibrils to be discovered. Our findings not only provide valuable insights into the structural roles of glycans in bio-assemblies but also demonstrate the potential of our recently formulated research strategy of CryoSeek to find bioentities and establish prototypes for structural studies of carbohydrates.
External linksProc Natl Acad Sci U S A / PubMed:39739783 / PubMed Central
MethodsEM (helical sym.)
Resolution3.5 Å
Structure data

60659

9ikm

EMDB-60659, PDB-9ikm:
Cryo-EM structure of TLP-4
Method: EM (helical sym.) / Resolution: 3.5 Å

Source
  • algae metagenome (others)
KeywordsPROTEIN FIBRIL / Fibril

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