1eok

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[[Image:1eok.jpg|left|200px]]<br /><applet load="1eok" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1eok.jpg|left|200px]]
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caption="1eok, resolution 1.80&Aring;" />
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'''CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F3'''<br />
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{{Structure
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|PDB= 1eok |SIZE=350|CAPTION= <scene name='initialview01'>1eok</scene>, resolution 1.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Mannosyl-glycoprotein_endo-beta-N-acetylglucosaminidase Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.96 3.2.1.96]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F3'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1EOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Mannosyl-glycoprotein_endo-beta-N-acetylglucosaminidase Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.96 3.2.1.96] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOK OCA].
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1EOK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOK OCA].
==Reference==
==Reference==
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Structural basis for the substrate specificity of endo-beta-N-acetylglucosaminidase F(3)., Waddling CA, Plummer TH Jr, Tarentino AL, Van Roey P, Biochemistry. 2000 Jul 11;39(27):7878-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10891067 10891067]
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Structural basis for the substrate specificity of endo-beta-N-acetylglucosaminidase F(3)., Waddling CA, Plummer TH Jr, Tarentino AL, Van Roey P, Biochemistry. 2000 Jul 11;39(27):7878-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10891067 10891067]
[[Category: Elizabethkingia meningoseptica]]
[[Category: Elizabethkingia meningoseptica]]
[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
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[[Category: alpha/beta-barrel]]
[[Category: alpha/beta-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:58:21 2008''

Revision as of 08:58, 20 March 2008


PDB ID 1eok

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands:
Activity: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase, with EC number 3.2.1.96
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE F3


Overview

Endo-beta-N-acetylglucosaminidase F(3) cleaves the beta(1-4) link between the core GlcNAc's of asparagine-linked oligosaccharides, with specificity for biantennary and triantennary complex glycans. The crystal structures of Endo F(3) and the complex with its reaction product, the biantennary octasaccharide, Gal-beta(1-4)-GlcNAc-beta(1-2)-Man-alpha(1-3)[Gal-beta(1-4)-GlcNAc-be ta(1-2)-Man-alpha(1-6)]-Man-beta(1-4)-GlcNAc, have been determined to 1.8 and 2.1 A resolution, respectively. Comparison of the structure of Endo F(3) with that of Endo F(1), which is specific for high-mannose oligosaccharides, reveals highly distinct folds and amino acid compositions at the oligosaccharide recognition sites. Binding of the oligosaccharide to the protein does not affect the protein conformation. The conformation of the oligosaccharide is similar to that seen for other biantennary oligosaccharides, with the exception of two links: the Gal-beta(1-4)-GlcNAc link of the alpha(1-3) branch and the GlcNAc-beta(1-2)-Man link of the alpha(1-6) branch. Especially the latter link is highly distorted and energetically unfavorable. Only the reducing-end GlcNAc and two Man's of the trimannose core are in direct contact with the protein. This is in contrast with biochemical data for Endo F(1) that shows that activity depends on the presence and identity of sugar residues beyond the trimannose core. The substrate specificity of Endo F(3) is based on steric exclusion of incompatible oligosaccharides rather than on protein-carbohydrate interactions that are unique to complexes with biantennary or triantennary complex glycans.

About this Structure

1EOK is a Single protein structure of sequence from Elizabethkingia meningoseptica. Full crystallographic information is available from OCA.

Reference

Structural basis for the substrate specificity of endo-beta-N-acetylglucosaminidase F(3)., Waddling CA, Plummer TH Jr, Tarentino AL, Van Roey P, Biochemistry. 2000 Jul 11;39(27):7878-85. PMID:10891067

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