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New page: left|200px<br /><applet load="1p4v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p4v, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1p4v.gif|left|200px]]<br /><applet load="1p4v" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1p4v, resolution 1.90&Aring;" />
'''CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT WITH GLYCINE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT WITH GLYCINE==
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.
<StructureSection load='1p4v' size='340' side='right'caption='[[1p4v]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1p4v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P4V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4v OCA], [https://pdbe.org/1p4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p4v RCSB], [https://www.ebi.ac.uk/pdbsum/1p4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p4v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ASPG_ELIMR ASPG_ELIMR] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. Requires that the glycosylated asparagine moiety is not substituted on its N-(R1) and C- (R2) terminus.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p4/1p4v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p4v ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1P4V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica] with GLY as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P4V OCA].
*[[Glycosylasparaginase|Glycosylasparaginase]]
 
__TOC__
==Reference==
</StructureSection>
A dual role for an aspartic acid in glycosylasparaginase autoproteolysis., Qian X, Guan C, Guo HC, Structure. 2003 Aug;11(8):997-1003. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12906830 12906830]
[[Category: Elizabethkingia meningoseptica]]
[[Category: Elizabethkingia meningoseptica]]
[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Guan C]]
[[Category: Guan, C.]]
[[Category: Guo HC]]
[[Category: Guo, H.C.]]
[[Category: Qian X]]
[[Category: Qian, X.]]
[[Category: GLY]]
[[Category: alpha beta]]
[[Category: beta alpha]]
[[Category: sandwich]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:28:36 2007''

Latest revision as of 08:05, 14 February 2024

CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT WITH GLYCINE

1p4v, resolution 1.90Å

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