1V6L

Peanut lectin-lactose complex in the presence of 9mer peptide (PVIWSSATG)

Summary for 1V6L

• Entry DOI: 10.2210/pdb1v6l/pdb
• Related: 1CR7 1V6I 1V6J 1V6K 1V6M 1V6N 1V6O 2PEL
• Related PRD ID: PRD_900004 PRD_900008
• Descriptor: Galactose-binding lectin, beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: lectin, open quaternary association, orthorhombic, carbohydrate specificity, protein crystallography, agglutinin, sugar binding protein
• Biological source: Arachis hypogaea (peanut)
• Total number of polymer chains: 4
• Total formula weight: 100574.79

Authors

Kundhavai Natchiar, S.,Arockia Jeyaprakash, A.,Ramya, T.N.C.,Thomas, C.J.,Suguna, K.,Surolia, A.,Vijayan, M. (deposition date: 2003-12-01, release date: 2004-02-10, Last modification date: 2023-12-27)

Primary citation

Kundhavai Natchiar, S.,Arockia Jeyaprakash, A.,Ramya, T.N.,Thomas, C.J.,Suguna, K.,Surolia, A.,Vijayan, M.
Structural plasticity of peanut lectin: an X-ray analysis involving variation in pH, ligand binding and crystal structure.
Acta Crystallogr.,Sect.D, 60:211-219, 2004

PubMed Abstract: Until recently, it has only been possible to grow crystals of peanut lectin when complexed with sugar ligands. It is now shown that it is possible to grow peanut lectin crystals at acidic pH in the presence of oligopeptides corresponding to a loop in the lectin molecule. Crystals have also been prepared in the presence of these peptides as well as lactose. Low-pH crystal forms of the lectin-lactose complex similar to those obtained at neutral pH have also been grown. Thus, crystals of peanut lectin grown under different environmental conditions, at two pH values with and without sugar bound to the lectin, are now available. They have been used to explore the plasticity and hydration of the molecule. A detailed comparison between different structures shows that the lectin molecule is sturdy and that the effect of changes in pH, ligand binding and environment on it is small. The region involving the curved front beta-sheet and the loops around the second hydrophobic core is comparatively rigid. The back beta-sheet involved in quaternary association, which exhibits considerable variability, is substantially flexible, as is the sugar-binding region. The numbers of invariant water molecules in the hydration shell are small and they are mainly involved in metal coordination or in stabilizing unusual structural features. Small consistent movements occur in the combining site upon sugar binding, although the site is essentially preformed.

PubMed: 14747696
DOI: 10.1107/S090744490302849X

Experimental method

X-RAY DIFFRACTION (2.5 Å)