1sfy

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(New page: 200px<br /><applet load="1sfy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sfy, resolution 2.55&Aring;" /> '''Crystal structure of...)
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[[Image:1sfy.gif|left|200px]]<br /><applet load="1sfy" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sfy.gif|left|200px]]<br /><applet load="1sfy" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1sfy, resolution 2.55&Aring;" />
caption="1sfy, resolution 2.55&Aring;" />
'''Crystal structure of recombinant Erythrina corallodandron Lectin'''<br />
'''Crystal structure of recombinant Erythrina corallodandron Lectin'''<br />
==Overview==
==Overview==
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The three-dimensional structure of the recombinant form of Erythrina, corallodendron lectin, complexed with lactose, has been elucidated by, X-ray crystallography at 2.55 A resolution. Comparison of this, non-glycosylated structure with that of the native glycosylated lectin, reveals that the tertiary and quaternary structures are identical in the, two forms, with local changes observed at one of the glycosylation sites, (Asn17). These changes take place in such a way that hydrogen bonds with, the neighboring protein molecules in rECorL compensate those made by the, glycan with the protein in ECorL. Contrary to an earlier report, this, study demonstrates that the glycan attached to the lectin does not, influence the oligomeric state of the lectin. Identical interactions, between the lectin and the non-covalently bound lactose in the two forms, indicate, in line with earlier reports, that glycosylation does not affect, the carbohydrate specificity of the lectin. The present study, the first, of its kind involving a glycosylated protein with a well-defined glycan, and the corresponding deglycosylated form, provides insights into the, structural aspects of protein glycosylation.
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The three-dimensional structure of the recombinant form of Erythrina corallodendron lectin, complexed with lactose, has been elucidated by X-ray crystallography at 2.55 A resolution. Comparison of this non-glycosylated structure with that of the native glycosylated lectin reveals that the tertiary and quaternary structures are identical in the two forms, with local changes observed at one of the glycosylation sites (Asn17). These changes take place in such a way that hydrogen bonds with the neighboring protein molecules in rECorL compensate those made by the glycan with the protein in ECorL. Contrary to an earlier report, this study demonstrates that the glycan attached to the lectin does not influence the oligomeric state of the lectin. Identical interactions between the lectin and the non-covalently bound lactose in the two forms indicate, in line with earlier reports, that glycosylation does not affect the carbohydrate specificity of the lectin. The present study, the first of its kind involving a glycosylated protein with a well-defined glycan and the corresponding deglycosylated form, provides insights into the structural aspects of protein glycosylation.
==About this Structure==
==About this Structure==
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1SFY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erythrina_corallodendron Erythrina corallodendron] with LAT, MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SFY OCA].
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1SFY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erythrina_corallodendron Erythrina corallodendron] with <scene name='pdbligand=LAT:'>LAT</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SFY OCA].
==Reference==
==Reference==
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[[Category: Erythrina corallodendron]]
[[Category: Erythrina corallodendron]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Kulkarni, K.A.]]
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[[Category: Kulkarni, K A.]]
[[Category: Mitra, N.]]
[[Category: Mitra, N.]]
[[Category: Srivastava, A.]]
[[Category: Srivastava, A.]]
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[[Category: legume lectin]]
[[Category: legume lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:21:32 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:05 2008''

Revision as of 13:01, 21 February 2008


1sfy, resolution 2.55Å

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Crystal structure of recombinant Erythrina corallodandron Lectin

Overview

The three-dimensional structure of the recombinant form of Erythrina corallodendron lectin, complexed with lactose, has been elucidated by X-ray crystallography at 2.55 A resolution. Comparison of this non-glycosylated structure with that of the native glycosylated lectin reveals that the tertiary and quaternary structures are identical in the two forms, with local changes observed at one of the glycosylation sites (Asn17). These changes take place in such a way that hydrogen bonds with the neighboring protein molecules in rECorL compensate those made by the glycan with the protein in ECorL. Contrary to an earlier report, this study demonstrates that the glycan attached to the lectin does not influence the oligomeric state of the lectin. Identical interactions between the lectin and the non-covalently bound lactose in the two forms indicate, in line with earlier reports, that glycosylation does not affect the carbohydrate specificity of the lectin. The present study, the first of its kind involving a glycosylated protein with a well-defined glycan and the corresponding deglycosylated form, provides insights into the structural aspects of protein glycosylation.

About this Structure

1SFY is a Single protein structure of sequence from Erythrina corallodendron with , and as ligands. Full crystallographic information is available from OCA.

Reference

Effect of glycosylation on the structure of Erythrina corallodendron lectin., Kulkarni KA, Srivastava A, Mitra N, Sharon N, Surolia A, Vijayan M, Suguna K, Proteins. 2004 Sep 1;56(4):821-7. PMID:15281133

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