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1p4k

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[[Image:1p4k.gif|left|200px]]
 
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==CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT==
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The line below this paragraph, containing "STRUCTURE_1p4k", creates the "Structure Box" on the page.
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<StructureSection load='1p4k' size='340' side='right'caption='[[1p4k]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1p4k| PDB=1p4k | SCENE= }}
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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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'''CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT'''
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==See Also==
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*[[Glycosylasparaginase|Glycosylasparaginase]]
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__TOC__
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==Overview==
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</StructureSection>
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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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==About this Structure==
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1P4K is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/12906830 12906830]
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[[Category: Elizabethkingia meningoseptica]]
[[Category: Elizabethkingia meningoseptica]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Guan, C.]]
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[[Category: Guan C]]
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[[Category: Guo, H C.]]
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[[Category: Guo HC]]
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[[Category: Qian, X.]]
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[[Category: Qian X]]
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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 Sat May 3 04:40:44 2008''
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Current revision

CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT

PDB ID 1p4k

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