PDBsum entry 1x1v

Sugar binding protein

PDB id: 1x1v

Contents

Protein chains

138 a.a. *

Ligands

MMA ×5

HEZ ×6

Metals

_ZN ×3

Waters ×498

* Residue conservation analysis

PDB id:

1x1v

Name:

Sugar binding protein

Title:

Structure of banana lectin- methyl-alpha-mannose complex

Structure:

Lectin. Chain: a, b

Source:

Musa acuminata. Organism_taxid: 4641. Other_details: synonym: musa paradisiaca

Resolution:

2.45Å R-factor: 0.226 R-free: 0.260

Authors:

D.D.Singh,K.Saikrishnan,P.Kumar,A.Surolia,K.Sekar,M.Vijayan

Key ref:

D.D.Singh et al. (2005). Unusual sugar specificity of banana lectin from Musa paradisiaca and its probable evolutionary origin. Crystallographic and modelling studies. Glycobiology, 15, 1025-1032. PubMed id: 15958419

Date:

14-Apr-05 Release date: 08-Nov-05

Protein chains

Q8L5H4  (Q8L5H4_MUSAC) -  Lectin from Musa acuminata

Seq: 141 a.a.

Struc: 138 a.a.

Glycobiology 15:1025-1032 (2005)

PubMed id: 15958419

Unusual sugar specificity of banana lectin from Musa paradisiaca and its probable evolutionary origin. Crystallographic and modelling studies.

D.D.Singh, K.Saikrishnan, P.Kumar, A.Surolia, K.Sekar, M.Vijayan.

ABSTRACT

The crystal structure of a complex of methyl-alpha-D-mannoside with banana lectin from Musa paradisiaca reveals two primary binding sites in the lectin, unlike in other lectins with beta-prism I fold which essentially consists of three Greek key motifs. It has been suggested that the fold evolved through successive gene duplication and fusion of an ancestral Greek key motif. In other lectins, all from dicots, the primary binding site exists on one of the three motifs in the three-fold symmetric molecule. Banana is a monocot, and the three motifs have not diverged enough to obliterate sequence similarity among them. Two Greek key motifs in it carry one primary binding site each. A common secondary binding site exists on the third Greek key. Modelling shows that both the primary sites can support 1-2, 1-3, and 1-6 linked mannosides with the second residue interacting in each case primarily with the secondary binding site. Modelling also readily leads to a bound branched mannopentose with the nonreducing ends of the two branches anchored at the two primary binding sites, providing a structural explanation for the lectin's specificity for branched alpha-mannans. A comparison of the dimeric banana lectin with other beta-prism I fold lectins, provides interesting insights into the variability in their quaternary structure.