2CYF

The Crystal Structure of Canavalia Maritima Lectin (ConM) in Complex with Trehalose and Maltose

Summary for 2CYF

• Entry DOI: 10.2210/pdb2cyf/pdb
• Related: 2CWM 2CY6
• Related PRD ID: PRD_900001
• Descriptor: Lectin, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: canacalia maritima, lectin, maltose, metal binding protein
• Biological source: Canavalia maritima
• Total number of polymer chains: 2
• Total formula weight: 51863.02

Authors

Delatorre, P.,Rocha, B.A.M.,Sousa, E.P.,Gadelha, C.A.A.,Azevedo Jr., W.F.,Cavada, B.S. (deposition date: 2005-07-06, release date: 2006-06-13, Last modification date: 2024-03-13)

Primary citation

Delatorre, P.,Rocha, B.A.M.,Gadelha, C.A.A.,Santi-Gadelha, T.,Cajazeiras, J.B.,Souza, E.P.,Nascimento, K.S.,Freire, V.N.,Sampaio, A.H.,Azevedo Jr., W.F.,Cavada, B.S.
Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins
J.Struct.Biol., 154:280-286, 2006

PubMed Abstract: The crystal structure of Canavalia maritima lectin (ConM) complexed with trehalose and maltose revealed relevant point mutations in ConA-like lectins. ConM with the disaccharides and other ConA-like lectins complexed with carbohydrates demonstrated significant differences in the position of H-bonds. The main difference in the ConM structure is the replacement of Pro202 by Ser202, a residue that promotes the approximation of Tyr12 to the carbohydrate-binding site. The O-6' of the second glucose ring in maltose interacts with Tyr12, while in trehalose the interaction is established by the O-2' and Tyr12, explaining the higher affinity of ConM for disaccharides compared to monosaccharides.

PubMed: 16677825
DOI: 10.1016/j.jsb.2006.03.011

Experimental method

X-RAY DIFFRACTION (1.8 Å)