5XZK

Pholiota squarrosa lectin trimer

Summary for 5XZK

• Entry DOI: 10.2210/pdb5xzk/pdb
• NMR Information: BMRB: 36103
• Descriptor: lectin (PhoSL) (1 entity in total)
• Functional Keywords: lectin, trimer, fucose, sugar binding protein
• Biological source: Pholiota squarrosa
• Total number of polymer chains: 3
• Total formula weight: 13322.87

Authors

Yamasaki, K. (deposition date: 2017-07-12, release date: 2018-06-06, Last modification date: 2024-05-01)

Primary citation

Yamasaki, K.,Yamasaki, T.,Tateno, H.
The trimeric solution structure and fucose-binding mechanism of the core fucosylation-specific lectin PhoSL.
Sci Rep, 8:7740-7740, 2018

PubMed Abstract: The core α1-6 fucosylation-specific lectin from a mushroom Pholiota squarrosa (PhoSL) is a potential tool for precise diagnosis of cancers. This lectin consists of only 40 amino acids and can be chemically synthesized. We showed here that a synthesized PhoSL peptide formed a trimer by gel filtration and chemical cross-linking assays, and determined a structure of the PhoSL trimer by NMR. The structure possesses a β-prism motif with a three-fold rotational symmetry, where three antiparallel β-sheets are tightly connected by swapping of β-strands. A triad of Trp residues comprises the structural core, forming NH-π electrostatic interactions among the indole rings. NMR analysis with an excess amount of fucose revealed the structural basis for the molecular recognition. Namely, fucose deeply enters a pocket formed at a junction of β-sheet edges, with the methyl group placed at the bottom. It forms a number of hydrophobic and hydrogen-bonding interactions with PhoSL residues. In spite of partial similarities to the structures of other functionally related lectins, the arrangement of the antiparallel β-sheets in the PhoSL trimer is novel as a structural scaffold, and thus defines a novel type of lectin structure.

PubMed: 29773815
DOI: 10.1038/s41598-018-25630-2

Experimental method

SOLUTION NMR