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1fx5
From Proteopedia
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'''CRYSTAL STRUCTURE ANALYSIS OF ULEX EUROPAEUS LECTIN I''' | '''CRYSTAL STRUCTURE ANALYSIS OF ULEX EUROPAEUS LECTIN I''' | ||
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[[Category: Delbaere, L T.J.]] | [[Category: Delbaere, L T.J.]] | ||
[[Category: Vandonselaar, M.]] | [[Category: Vandonselaar, M.]] | ||
| - | [[Category: | + | [[Category: Fucose specific lectin]] |
| - | [[Category: | + | [[Category: Homo-dimer]] |
| - | [[Category: | + | [[Category: Legume lectin]] |
| - | [[Category: | + | [[Category: Ue-i]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:52:01 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:52, 2 May 2008
CRYSTAL STRUCTURE ANALYSIS OF ULEX EUROPAEUS LECTIN I
Overview
The tertiary and quaternary structure of the lectin I from Ulex europaeus (UE-I) has been determined to 2.2 A resolution. UE-I is a dimeric metalloglycoprotein that binds the H-type 2 human blood group determinant [alpha-L-Fucalpha(1-->2)-beta-D-Galbeta(1-->4)-beta-D-Glc NAcalpha-]. Nine changes from the published amino acid sequence were necessary to account for the electron density. The quaternary structural organization of UE-I is that of the most commonly occurring legume lectin dimer. The tertiary structure of the monomeric subunits is similar to that in the conventional lectin subunit; however, some structural differences are noted. These differences include a four-stranded anti-parallel "S" sheet in UE-I versus the five-stranded S sheet in other lectin monomers. The Ala residue of the Ala-Asp cis-peptide bond present in the carbohydrate-binding site of the conventional lectin monomer is replaced with a Thr in the UE-I structure. Also, a novel disulfide bridge linking Cys115 and Cys150 is present. There are two metallic ions, one calcium and the other manganese, per subunit. N-linked oligosaccharides are at residues 23 and 111 of each subunit. One molecule of R-2-methyl-2, 4-pentanediol (R-MPD) is present in a shallow depression on the surface of each subunit. In order to examine the binding of the H-type 2 blood group determinant by UE-I, its beta-methyl glycoside (H-type 2-OMe) was docked into the binding site of R-MPD. The epitope previously identified for H-type 2-OMe by chemical mapping proved, with only minor adjustment of amino acid residues, to be complementary to the shallow cavity occupied by R-MPD in the structure. Several key interactions have been proposed between the H-type 2-OMe and UE-I.
About this Structure
1FX5 is a Single protein structure of sequence from Ulex europaeus. Full crystallographic information is available from OCA.
Reference
The 2.2 A resolution structure of the O(H) blood-group-specific lectin I from Ulex europaeus., Audette GF, Vandonselaar M, Delbaere LT, J Mol Biol. 2000 Dec 1;304(3):423-33. PMID:11090284 Page seeded by OCA on Fri May 2 16:52:01 2008
