1DLP

STRUCTURAL CHARACTERIZATION OF THE NATIVE FETUIN-BINDING PROTEIN SCILLA CAMPANULATA AGGLUTININ (SCAFET): A NOVEL TWO-DOMAIN LECTIN

Summary for 1DLP

• Entry DOI: 10.2210/pdb1dlp/pdb
• Related: 1B2P
• Descriptor: LECTIN SCAFET PRECURSOR (2 entities in total)
• Functional Keywords: two-domain lectin, beta prism ii fold, native, sugar binding protein
• Biological source: Hyacinthoides hispanica
• Total number of polymer chains: 6
• Total formula weight: 153272.26

Authors

Wright, L.M.,Reynolds, C.D.,Rizkallah, P.J.,Allen, A.K.,VanDamme, E.J.M.,Donovan, M.J.,Peumans, W.J. (deposition date: 1999-12-11, release date: 2000-02-10, Last modification date: 2024-10-30)

Primary citation

Wright, L.M.,Reynolds, C.D.,Rizkallah, P.J.,Allen, A.K.,Van Damme, E.J.,Donovan, M.J.,Peumans, W.J.
Structural characterisation of the native fetuin-binding protein Scilla campanulata agglutinin: a novel two-domain lectin.
FEBS Lett., 468:19-22, 2000

PubMed Abstract: The three-dimensional structure of a 244-residue, multivalent, fetuin-binding lectin, SCAfet, isolated from bluebell (Scilla campanulata) bulbs, has been solved at 3.3 A resolution by molecular replacement using the coordinates of the 119-residue, mannose-binding lectin, SCAman, also from bluebell bulbs. Unlike most monocot mannose-binding lectins, such as Galanthus nivalis agglutinin from snowdrop bulbs, which fold into a single domain, SCAfet contains two domains with approximately 55% sequence identity, joined by a linker peptide. Both domains are made up of a 12-stranded beta-prism II fold, with three putative carbohydrate-binding sites, one on each subdomain. SCAfet binds to the complex saccharides of various animal glycoproteins but not to simple sugars.

PubMed: 10683433
DOI: 10.1016/S0014-5793(00)01109-1

Experimental method

X-RAY DIFFRACTION (3.3 Å)