1fx5

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|PDB= 1fx5 |SIZE=350|CAPTION= <scene name='initialview01'>1fx5</scene>, resolution 2.2&Aring;
|PDB= 1fx5 |SIZE=350|CAPTION= <scene name='initialview01'>1fx5</scene>, resolution 2.2&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XYL:D-XYLITOL'>XYL</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fx5 OCA], [http://www.ebi.ac.uk/pdbsum/1fx5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fx5 RCSB]</span>
}}
}}
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[[Category: Delbaere, L T.J.]]
[[Category: Delbaere, L T.J.]]
[[Category: Vandonselaar, M.]]
[[Category: Vandonselaar, M.]]
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[[Category: CA]]
 
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[[Category: MN]]
 
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[[Category: MRD]]
 
[[Category: fucose specific lectin]]
[[Category: fucose specific lectin]]
[[Category: homo-dimer]]
[[Category: homo-dimer]]
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[[Category: ue-i]]
[[Category: ue-i]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:15:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:32:05 2008''

Revision as of 17:32, 30 March 2008


PDB ID 1fx5

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: , , , , , , ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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