1p4k

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[[Image:1p4k.gif|left|200px]]<br /><applet load="1p4k" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1p4k, resolution 1.90&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT==
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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.
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<StructureSection load='1p4k' size='340' side='right'caption='[[1p4k]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1p4k]] 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=1P4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P4K FirstGlance]. <br>
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4k OCA], [https://pdbe.org/1p4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p4k RCSB], [https://www.ebi.ac.uk/pdbsum/1p4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p4k ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p4/1p4k_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1p4k ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1P4K 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 <scene name='pdbligand=GOL:'>GOL</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4K OCA].
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*[[Glycosylasparaginase|Glycosylasparaginase]]
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__TOC__
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==Reference==
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</StructureSection>
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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]
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[[Category: Elizabethkingia meningoseptica]]
[[Category: Elizabethkingia meningoseptica]]
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[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Guan C]]
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[[Category: Guan, C.]]
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[[Category: Guo HC]]
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[[Category: Guo, H C.]]
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[[Category: Qian X]]
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[[Category: Qian, X.]]
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[[Category: GOL]]
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[[Category: alpha beta]]
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[[Category: beta alpha]]
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[[Category: sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:00 2008''
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Current revision

CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT

PDB ID 1p4k

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