3R0E

Structure of Remusatia vivipara lectin

Summary for 3R0E

• Entry DOI: 10.2210/pdb3r0e/pdb
• Related: 1DLP 1KJ1 1MSA
• Descriptor: Lectin (3 entities in total)
• Functional Keywords: carbohydrate binding, carbohydrate, sugar binding protein
• Biological source: Remusatia vivipara; More
• Total number of polymer chains: 4
• Total formula weight: 48345.79

Authors

Shetty, K.N.,Bhat, G.G.,Swamy, B.M.,Suguna, K. (deposition date: 2011-03-07, release date: 2011-08-10, Last modification date: 2024-11-20)

Primary citation

Shetty, K.N.,Bhat, G.G.,Inamdar, S.R.,Swamy, B.M.,Suguna, K.
Crystal structure of a {beta}-prism II lectin from Remusatia vivipara.
Glycobiology, 22:56-69, 2012

PubMed Abstract: The crystal structure of a β-prism II (BP2) fold lectin from Remusatia vivipara, a plant of traditional medicinal value, has been determined at a resolution of 2.4 Å. This lectin (RVL, Remusatia vivipara lectin) is a dimer with each protomer having two distinct BP2 domains without a linker between them. It belongs to the "monocot mannose-binding" lectin family, which consists of proteins of high sequence and structural similarity. Though the overall tertiary structure is similar to that of lectins from snowdrop bulbs and garlic, crucial differences in the mannose-binding regions and oligomerization were observed. Unlike most of the other structurally known proteins in this family, only one of the three carbohydrate recognition sites (CRSs) per BP2 domain is found to be conserved. RVL does not recognize simple mannose moieties. RVL binds to only N-linked complex glycans like those present on the gp120 envelope glycoprotein of HIV and mannosylated blood proteins like fetuin, but not to simple mannose moieties. The molecular basis for these features and their possible functional implications to understand the different levels of carbohydrate affinities in this structural family have been investigated through structure analysis, modeling and binding studies. Apart from being the first structure of a lectin to be reported from the Araceae/Arum family, this protein also displays a novel mode of oligomerization among BP2 lectins.

PubMed: 21788359
DOI: 10.1093/glycob/cwr100

Experimental method

X-RAY DIFFRACTION (2.4 Å)