2gl9
From Proteopedia
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|PDB= 2gl9 |SIZE=350|CAPTION= <scene name='initialview01'>2gl9</scene>, resolution 2.00Å | |PDB= 2gl9 |SIZE=350|CAPTION= <scene name='initialview01'>2gl9</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ASN:ASPARAGINE'>ASN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
| - | |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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Guo, H C.]] | [[Category: Guo, H C.]] | ||
[[Category: Wang, Y.]] | [[Category: Wang, Y.]] | ||
| - | [[Category: ASN]] | ||
| - | [[Category: NAG]] | ||
[[Category: catalytic mechanism]] | [[Category: catalytic mechanism]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
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[[Category: proton-relay network]] | [[Category: proton-relay network]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:18:10 2008'' |
Revision as of 00:18, 31 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 03:18:10 2008
Categories: Elizabethkingia meningoseptica | N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase | Protein complex | Guo, H C. | Wang, Y. | Catalytic mechanism | Crystal structure | Electron-pair transfer | Enzyme-acyl intermediate | Enzyme-substrate complex | Glycosylasparaginase | Ntn-hydrolase | Nucleophilic attack | Oxyanion hole | Proton-relay network
