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2gl9

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[[Image:2gl9.gif|left|200px]]
[[Image:2gl9.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2gl9 |SIZE=350|CAPTION= <scene name='initialview01'>2gl9</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_2gl9", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ASN:ASPARAGINE'>ASN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2gl9| PDB=2gl9 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gl9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gl9 OCA], [http://www.ebi.ac.uk/pdbsum/2gl9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gl9 RCSB]</span>
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}}
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'''Crystal Structure of Glycosylasparaginase-Substrate Complex'''
'''Crystal Structure of Glycosylasparaginase-Substrate Complex'''
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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]
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]]
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[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
 
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Guo, H C.]]
[[Category: Guo, H C.]]
[[Category: Wang, Y.]]
[[Category: Wang, Y.]]
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[[Category: catalytic mechanism]]
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[[Category: Catalytic mechanism]]
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[[Category: crystal structure]]
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[[Category: Crystal structure]]
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[[Category: electron-pair transfer]]
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[[Category: Electron-pair transfer]]
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[[Category: enzyme-acyl intermediate]]
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[[Category: Enzyme-acyl intermediate]]
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[[Category: enzyme-substrate complex]]
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[[Category: Enzyme-substrate complex]]
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[[Category: glycosylasparaginase]]
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[[Category: Glycosylasparaginase]]
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[[Category: ntn-hydrolase]]
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[[Category: Ntn-hydrolase]]
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[[Category: nucleophilic attack]]
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[[Category: Nucleophilic attack]]
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[[Category: oxyanion hole]]
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[[Category: Oxyanion hole]]
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[[Category: proton-relay network]]
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[[Category: Proton-relay network]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:13:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:18:10 2008''
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Revision as of 02:13, 4 May 2008

Image:2gl9.gif

Template:STRUCTURE 2gl9

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 Page seeded by OCA on Sun May 4 05:13:46 2008

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