3A5P

Crystal structure of hemagglutinin

Summary for 3A5P

• Entry DOI: 10.2210/pdb3a5p/pdb
• Descriptor: Haemagglutinin I (2 entities in total)
• Functional Keywords: lectin, sugar binding protein
• Biological source: Physarum polycephalum (Slime mold)
• Total number of polymer chains: 4
• Total formula weight: 43600.40

Authors

Watanabe, N.,Sakai, N.,Nakamura, T.,Nabeshima, Y.,Kouno, T.,Mizuguchi, M.,Kawano, K. (deposition date: 2009-08-10, release date: 2010-08-11, Last modification date: 2024-04-03)

Primary citation

Kouno, T.,Watanabe, N.,Sakai, N.,Nakamura, T.,Nabeshima, Y.,Morita, M.,Mizuguchi, M.,Aizawa, T.,Demura, M.,Imanaka, T.,Tanaka, I.,Kawano, K.
The Structure of Physarum polycephalum hemagglutinin I suggests a minimal carbohydrate recognition domain of legume lectin fold
J.Mol.Biol., 405:560-569, 2011

PubMed Abstract: Physarum polycephalum hemagglutinin I (HA1) is a 104-residue protein that is secreted to extracellular space. The crystal structure of HA1 has a β-sandwich fold found among lectin structures, such as legume lectins and galectins. Interestingly, the β-sandwich of HA1 lacks a jelly roll motif and is essentially composed of two simple up-and-down β-sheets. This up-and-down β-sheet motif is well conserved in other legume lectin-like proteins derived from animals, plants, bacteria, and viruses. It is more noteworthy that the up-and-down β-sheet motif includes many residues that make contact with the target carbohydrates. Our NMR data demonstrate that HA1 lacking a jelly roll motif also binds to its target glycopeptide. Taken together, these data show that the up-and-down β-sheet motif provides a fundamental scaffold for the binding of legume lectin-like proteins to the target carbohydrates, and the structure of HA1 suggests a minimal carbohydrate recognition domain.

PubMed: 21094650
DOI: 10.1016/j.jmb.2010.11.024

Experimental method

X-RAY DIFFRACTION (1.82 Å)