1p4v
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GLY:GLYCINE'>GLY</scene> | |LIGAND= <scene name='pdbligand=GLY:GLYCINE'>GLY</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=[[1p4k|1P4K]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4v OCA], [http://www.ebi.ac.uk/pdbsum/1p4v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p4v RCSB]</span> | ||
}} | }} | ||
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[[Category: Guo, H C.]] | [[Category: Guo, H C.]] | ||
[[Category: Qian, X.]] | [[Category: Qian, X.]] | ||
| - | [[Category: GLY]] | ||
[[Category: alpha beta]] | [[Category: alpha beta]] | ||
[[Category: beta alpha]] | [[Category: beta alpha]] | ||
[[Category: sandwich]] | [[Category: sandwich]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:54:50 2008'' |
Revision as of 19:54, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26 | ||||||
| Related: | 1P4K
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT WITH GLYCINE
Overview
Glycosylasparaginase uses an autoproteolytic processing mechanism, through an N-O acyl shift, to generate a mature/active enzyme from a single-chain precursor. Structures of glycosylasparaginase precursors in complex with a glycine inhibitor have revealed the backbone in the immediate vicinity of the scissile peptide bond to be in a distorted trans conformation, which is believed to be the driving force for the N-O acyl shift to break the peptide bond. Here we report the effects of point mutation D151N. In addition to the loss of the base essential in autoproteolysis, this mutation also eradicates the backbone distortion near the scissile peptide bond. Binding of the glycine inhibitor to the autoproteolytic site of the D151N mutant does not restore the backbone distortion. Therefore, Asp151 plays a dual role, acting as the general base to activate the nucleophile and holding the distorted trans conformation that is critical for initiating an N-O acyl shift.
About this Structure
1P4V is a Single protein structure of sequence from Elizabethkingia meningoseptica. Full crystallographic information is available from OCA.
Reference
A dual role for an aspartic acid in glycosylasparaginase autoproteolysis., Qian X, Guan C, Guo HC, Structure. 2003 Aug;11(8):997-1003. PMID:12906830
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