2gl9

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[[Image:2gl9.gif|left|200px]]<br /><applet load="2gl9" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2gl9.gif|left|200px]]
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caption="2gl9, resolution 2.00&Aring;" />
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'''Crystal Structure of Glycosylasparaginase-Substrate Complex'''<br />
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{{Structure
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|PDB= 2gl9 |SIZE=350|CAPTION= <scene name='initialview01'>2gl9</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=ASN:ASPARAGINE'>ASN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26]
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|GENE=
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}}
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'''Crystal Structure of Glycosylasparaginase-Substrate Complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2GL9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=ASN:'>ASN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GL9 OCA].
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2GL9 is a [[Protein complex]] structure of sequences 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=2GL9 OCA].
==Reference==
==Reference==
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Crystallographic snapshot of a productive glycosylasparaginase-substrate complex., Wang Y, Guo HC, J Mol Biol. 2007 Feb 9;366(1):82-92. Epub 2006 Sep 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17157318 17157318]
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Crystallographic snapshot of a productive glycosylasparaginase-substrate complex., Wang Y, Guo HC, J Mol Biol. 2007 Feb 9;366(1):82-92. Epub 2006 Sep 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17157318 17157318]
[[Category: Elizabethkingia meningoseptica]]
[[Category: Elizabethkingia meningoseptica]]
[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
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[[Category: proton-relay network]]
[[Category: proton-relay network]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:06:04 2008''

Revision as of 15:06, 20 March 2008

Image:2gl9.gif


PDB ID 2gl9

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: and
Activity: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Glycosylasparaginase-Substrate Complex


Overview

Glycosylasparaginase (GA) plays an important role in asparagine-linked glycoprotein degradation. A deficiency in the activity of human GA leads to a lysosomal storage disease named aspartylglycosaminuria. GA belongs to a superfamily of N-terminal nucleophile hydrolases that autoproteolytically generate their mature enzymes from inactive single chain protein precursors. The side-chain of the newly exposed N-terminal residue then acts as a nucleophile during substrate hydrolysis. By taking advantage of mutant enzyme of Flavobacterium meningosepticum GA with reduced enzymatic activity, we have obtained a crystallographic snapshot of a productive complex with its substrate (NAcGlc-Asn), at 2.0 A resolution. This complex structure provided us an excellent model for the Michaelis complex to examine the specific contacts critical for substrate binding and catalysis. Substrate binding induces a conformational change near the active site of GA. To initiate catalysis, the side-chain of the N-terminal Thr152 is polarized by the free alpha-amino group on the same residue, mediated by the side-chain hydroxyl group of Thr170. Cleavage of the amide bond is then accomplished by a nucleophilic attack at the carbonyl carbon of the amide linkage in the substrate, leading to the formation of an acyl-enzyme intermediate through a negatively charged tetrahedral transition state.

About this Structure

2GL9 is a Protein complex structure of sequences from Elizabethkingia meningoseptica. Full crystallographic information is available from OCA.

Reference

Crystallographic snapshot of a productive glycosylasparaginase-substrate complex., Wang Y, Guo HC, J Mol Biol. 2007 Feb 9;366(1):82-92. Epub 2006 Sep 26. PMID:17157318

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