1MSA

MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM SNOWDROP (GALANTHUS NIVALIS) BULBS COMPLEXED WITH METHYL-ALPHA-D-MANNOSIDE

Summary for 1MSA

• Entry DOI: 10.2210/pdb1msa/pdb
• Descriptor: AGGLUTININ, methyl alpha-D-mannopyranoside (3 entities in total)
• Functional Keywords: methyl-alpha-d-mannoside, lectin (agglutinin)
• Biological source: Galanthus nivalis (common snowdrop)
• Cellular location: Secreted (By similarity): P30617
• Total number of polymer chains: 4
• Total formula weight: 50575.58

Authors

Wright, C.S.,Hester, G. (deposition date: 1995-03-06, release date: 1995-09-15, Last modification date: 2024-10-30)

Primary citation

Hester, G.,Kaku, H.,Goldstein, I.J.,Wright, C.S.
Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family.
Nat.Struct.Biol., 2:472-479, 1995

PubMed Abstract: Tetrameric Galanthus nivalis agglutinin (50,000 M(r)) belongs to a super-family of alpha-D-mannose-specific plant bulb lectins known to be potent inhibitors of retroviruses. The 2.3 A crystal structure of this lectin complexed with methyl alpha-D-mannose reveals a novel three-fold symmetric beta-sheet polypeptide fold. Three antiparallel four-stranded beta-sheets, each with a conserved mannose-binding site, are arranged as a 12-stranded beta-barrel. The tetramer displays 222 symmetry. Pairs of monomers form stable dimers through C-terminal strand exchange. The so formed hybrid beta-sheets are the sites for high affinity mannose binding in the dimer interface. Occupancy observed at corresponding sites in other beta-sheets suggests a potential for twelve sites per tetramer.

PubMed: 7664110
DOI: 10.1038/nsb0695-472

Experimental method

X-RAY DIFFRACTION (2.29 Å)