3WMQ

Crystal structure of the complex between SLL-2 and GalNAc.

Summary for 3WMQ

• Entry DOI: 10.2210/pdb3wmq/pdb
• Related: 3WMP
• Descriptor: Galactose-binding lectin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-alpha-D-galactopyranose, ... (7 entities in total)
• Functional Keywords: six-stranded antiparallel-beta sandwich, galactose binding protein, sugar binding protein
• Biological source: Sinularia lochmodes
• Total number of polymer chains: 1
• Total formula weight: 11842.76

Authors

Kita, A.,Jimbo, M.,Sakai, R.,Morimoto, Y.,Miki, K. (deposition date: 2013-11-22, release date: 2015-01-14, Last modification date: 2023-11-08)

Primary citation

Kita, A.,Jimbo, M.,Sakai, R.,Morimoto, Y.,Miki, K.
Crystal structure of a symbiosis-related lectin from octocoral.
Glycobiology, 25:1016-1023, 2015

PubMed Abstract: D-Galactose-binding lectin from the octocoral, Sinularia lochmodes (SLL-2), distributes densely on the cell surface of microalgae, Symbiodinium sp., an endosymbiotic dinoflagellate of the coral, and is also shown to be a chemical cue that transforms dinoflagellate into a non-motile (coccoid) symbiotic state. SLL-2 binds with high affinity to the Forssman antigen (N-acetylgalactosamine(GalNAc)α1-3GalNAcβ1-3Galα1-4Galβ1-4Glc-ceramide), and the presence of Forssman antigen-like sugar on the surface of Symbiodinium CS-156 cells was previously confirmed. Here we report the crystal structures of SLL-2 and its GalNAc complex as the first crystal structures of a lectin involved in the symbiosis between coral and dinoflagellate. N-Linked sugar chains and a galactose derivative binding site common to H-type lectins were observed in each monomer of the hexameric SLL-2 crystal structure. In addition, unique sugar-binding site-like regions were identified at the top and bottom of the hexameric SLL-2 structure. These structural features suggest a possible binding mode between SLL-2 and Forssman antigen-like pentasaccharide.

PubMed: 26022515
DOI: 10.1093/glycob/cwv033

Experimental method

X-RAY DIFFRACTION (1.6 Å)