1cjp
From Proteopedia
|
CONCANAVALIN A COMPLEX WITH 4'-METHYLUMBELLIFERYL-ALPHA-D-GLUCOPYRANOSIDE
Overview
Concanavalin A (Con A) is the best known plant lectin, with important, biological properties arising from its specific saccharide-binding, ability. Its exact biological role still remains unknown. The complex of, Con A with 4'-methylumbelliferyl-alpha-D-glucopyranoside (alpha-MUG) has, been crystallized in space group P2(1) with cell dimensions a = 81.62 A, b, = 128.71 A, c = 82.23 A, and beta = 118.47 degrees. X-ray diffraction, intensities to 2.78 A have been collected. The structure of the complex, was solved by molecular replacement and refined by simulated annealing, methods to a crystallographic R-factor value of 0.182 and a free-R-factor, value of 0.216. The asymmetric unit contains four subunits arranged as a, tetramer, with approximate 222 symmetry. A saccharide molecule is bound in, the sugar-binding site at the surface of each subunit, with the nonsugar, (aglycon) part adopting a different orientation in each subunit. The, aglycon orientation, although probably determined by packing of tetramers, in the crystal lattice, helps to characterize the orientation of the, saccharide in the sugar-binding pocket. The structure is the best, determined alpha-D-glucoside:Con A complex to date and the hydrogen, bonding network in the saccharide-binding site can be described with some, confidence and compared with that of the alpha-D-mannosides.
About this Structure
1CJP is a Single protein structure of sequence from Canavalia ensiformis with MUG, MN and CA as ligands. Full crystallographic information is available from OCA.
Reference
The crystal structure of the complex of concanavalin A with 4'-methylumbelliferyl-alpha-D-glucopyranoside., Hamodrakas SJ, Kanellopoulos PN, Pavlou K, Tucker PA, J Struct Biol. 1997 Feb;118(1):23-30. PMID:9087912
Page seeded by OCA on Tue Nov 20 12:31:01 2007
