2cbi

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[[Image:2cbi.gif|left|200px]]<br /><applet load="2cbi" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2cbi.gif|left|200px]]
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caption="2cbi, resolution 2.25&Aring;" />
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'''STRUCTURE OF THE CLOSTRIDIUM PERFRINGENS NAGJ FAMILY 84 GLYCOSIDE HYDROLASE, A HOMOLOGUE OF HUMAN O-GLCNACASE'''<br />
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{{Structure
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|PDB= 2cbi |SIZE=350|CAPTION= <scene name='initialview01'>2cbi</scene>, resolution 2.25&Aring;
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=GBL:GAMMA-BUTYROLACTONE'>GBL</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Hyalurononglucosaminidase Hyalurononglucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35]
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|GENE=
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}}
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'''STRUCTURE OF THE CLOSTRIDIUM PERFRINGENS NAGJ FAMILY 84 GLYCOSIDE HYDROLASE, A HOMOLOGUE OF HUMAN O-GLCNACASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2CBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=GBL:'>GBL</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hyalurononglucosaminidase Hyalurononglucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CBI OCA].
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2CBI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CBI OCA].
==Reference==
==Reference==
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Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis., Rao FV, Dorfmueller HC, Villa F, Allwood M, Eggleston IM, van Aalten DM, EMBO J. 2006 Apr 5;25(7):1569-78. Epub 2006 Mar 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16541109 16541109]
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Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis., Rao FV, Dorfmueller HC, Villa F, Allwood M, Eggleston IM, van Aalten DM, EMBO J. 2006 Apr 5;25(7):1569-78. Epub 2006 Mar 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16541109 16541109]
[[Category: Clostridium perfringens]]
[[Category: Clostridium perfringens]]
[[Category: Hyalurononglucosaminidase]]
[[Category: Hyalurononglucosaminidase]]
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[[Category: SO4]]
[[Category: SO4]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: carbohydrates]]
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[[Category: carbohydrate]]
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[[Category: family 84 glycoside hydrolases]]
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[[Category: family 84 glycoside hydrolase]]
[[Category: glycoside hydrolase]]
[[Category: glycoside hydrolase]]
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[[Category: hyaluronidases]]
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[[Category: hyaluronidase]]
[[Category: hydrolase]]
[[Category: hydrolase]]
[[Category: o-glcnac]]
[[Category: o-glcnac]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:13:18 2008''

Revision as of 14:13, 20 March 2008

Image:2cbi.gif


PDB ID 2cbi

Drag the structure with the mouse to rotate
, resolution 2.25Å
Sites:
Ligands: , , , and
Activity: Hyalurononglucosaminidase, with EC number 3.2.1.35
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE CLOSTRIDIUM PERFRINGENS NAGJ FAMILY 84 GLYCOSIDE HYDROLASE, A HOMOLOGUE OF HUMAN O-GLCNACASE


Overview

O-linked N-acetylglucosamine (O-GlcNAc) modification of specific serines/threonines on intracellular proteins in higher eukaryotes has been shown to directly regulate important processes such as the cell cycle, insulin sensitivity and transcription. The structure, molecular mechanisms of catalysis, protein substrate recognition/specificity of the eukaryotic O-GlcNAc transferase and hydrolase are largely unknown. Here we describe the crystal structure, enzymology and in vitro activity on human substrates of Clostridium perfringens NagJ, a close homologue of human O-GlcNAcase (OGA), representing the first family 84 glycoside hydrolase structure. The structure reveals a deep active site pocket highly conserved with the human enzyme, compatible with binding of O-GlcNAcylated peptides. Together with mutagenesis data, the structure supports a variant of the substrate-assisted catalytic mechanism, involving two aspartic acids and an unusually positioned tyrosine. Insights into recognition of substrate come from a complex with the transition state mimic O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (Ki=5.4 nM). Strikingly, the enzyme is inhibited by the pseudosubstrate peptide Ala-Cys(-S-GlcNAc)-Ala, and has OGA activity against O-GlcNAcylated human proteins, suggesting that the enzyme is a suitable model for further studies into the function of human OGA.

About this Structure

2CBI is a Single protein structure of sequence from Clostridium perfringens. Full crystallographic information is available from OCA.

Reference

Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis., Rao FV, Dorfmueller HC, Villa F, Allwood M, Eggleston IM, van Aalten DM, EMBO J. 2006 Apr 5;25(7):1569-78. Epub 2006 Mar 16. PMID:16541109

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