1fx5
From Proteopedia
(New page: 200px<br /><applet load="1fx5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fx5, resolution 2.2Å" /> '''CRYSTAL STRUCTURE ANA...) |
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| - | [[Image:1fx5.gif|left|200px]]<br /><applet load="1fx5" size=" | + | [[Image:1fx5.gif|left|200px]]<br /><applet load="1fx5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fx5, resolution 2.2Å" /> | caption="1fx5, resolution 2.2Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF ULEX EUROPAEUS LECTIN I'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF ULEX EUROPAEUS LECTIN I'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The tertiary and quaternary structure of the lectin I from Ulex europaeus | + | 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== | ==About this Structure== | ||
| - | 1FX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ulex_europaeus Ulex europaeus] with MN, CA and MRD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FX5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ulex_europaeus Ulex europaeus] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MRD:'>MRD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FX5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ulex europaeus]] | [[Category: Ulex europaeus]] | ||
| - | [[Category: Audette, G | + | [[Category: Audette, G F.]] |
| - | [[Category: Delbaere, L | + | [[Category: Delbaere, L T.J.]] |
[[Category: Vandonselaar, M.]] | [[Category: Vandonselaar, M.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: ue-i]] | [[Category: ue-i]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:42 2008'' |
Revision as of 10:43, 21 February 2008
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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 with , and as ligands. 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 Thu Feb 21 12:43:42 2008
Categories: Single protein | Ulex europaeus | Audette, G F. | Delbaere, L T.J. | Vandonselaar, M. | CA | MN | MRD | Fucose specific lectin | Homo-dimer | Legume lectin | Ue-i
