2bp6

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spinqualitylabelsall models 2bp6, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF PSEUDOMONAS AERUGINOSA LECTIN (PA-IIL) COMPLEXED WITH A-L-GALACTOPYRANOSIDE

Overview

The lectin from Pseudomonas aeruginosa (PA-IIL) is involved in host, recognition and biofilm formation. Lectin not only displays an unusually, high affinity for fucose but also binds to L-fucose, L-galactose and, D-arabinose that differ only by the group at position 5 of the sugar ring., Isothermal calorimetry experiments provided precise determination of, affinity for the three methyl-glycosides and revealed a large enthalpy, contribution. The crystal structures of the complexes of PA-IIL with, L-galactose and Met-beta-D-arabinoside have been determined and compared, with the PA-IIL/fucose complex described previously. A combination of the, structures and thermodynamics provided clues for the role of the, hydrophobic group in affinity.

About this Structure

2BP6 is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with GXL, CA and SO4 as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: thermodynamics data correlated with X-ray structures., Sabin C, Mitchell EP, Pokorna M, Gautier C, Utille JP, Wimmerova M, Imberty A, FEBS Lett. 2006 Feb 6;580(3):982-7. Epub 2006 Jan 19. PMID:16438968

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