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2gak

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(New page: 200px<br /><applet load="2gak" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gak, resolution 2.0&Aring;" /> '''X-ray crystal structu...)
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[[Image:2gak.gif|left|200px]]<br /><applet load="2gak" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2gak, resolution 2.0&Aring;" />
 
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'''X-ray crystal structure of murine leukocyte-type Core 2 b1,6-N-acetylglucosaminyltransferase (C2GnT-L)'''<br />
 
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==Overview==
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==X-ray crystal structure of murine leukocyte-type Core 2 b1,6-N-acetylglucosaminyltransferase (C2GnT-L)==
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Leukocyte type core 2 beta1,6-N-acetylglucosaminyltransferase (C2GnT-L) is, a key enzyme in the biosynthesis of branched O-glycans. It is an, inverting, metal ion-independent family 14 glycosyltransferase that, catalyzes the formation of the core 2 O-glycan, (Galbeta1-3[GlcNAcbeta1-6]GalNAc-O-Ser/Thr) from its donor and acceptor, substrates, UDP-GlcNAc and the core 1 O-glycan, (Galbeta1-3GalNAc-O-Ser/Thr), respectively. Reported here are the x-ray, crystal structures of murine C2GnT-L in the absence and presence of the, acceptor substrate Galbeta1-3GalNAc at 2.0 and 2.7A resolution, respectively. C2GnT-L was found to possess the GT-A fold; however, it, lacks the characteristic metal ion binding DXD motif. The Galbeta1-3GalNAc, complex defines the determinants of acceptor substrate binding and shows, that Glu-320 corresponds to the structurally conserved catalytic base, found in other inverting GT-A fold glycosyltransferases. Comparison of the, C2GnT-L structure with that of other GT-A fold glycosyltransferases, further suggests that Arg-378 and Lys-401 serve to electrostatically, stabilize the nucleoside diphosphate leaving group, a role normally played, by metal ion in GT-A structures. The use of basic amino acid side chains, in this way is strikingly similar to that seen in a number of metal, ion-independent GT-B fold glycosyltransferases and suggests a convergence, of catalytic mechanism shared by both GT-A and GT-B fold, glycosyltransferases.
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<StructureSection load='2gak' size='340' side='right'caption='[[2gak]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2gak]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GAK 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]] 2&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2gak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gak OCA], [https://pdbe.org/2gak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gak RCSB], [https://www.ebi.ac.uk/pdbsum/2gak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gak ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GCNT1_MOUSE GCNT1_MOUSE] Forms critical branches in O-glycans.<ref>PMID:7983056</ref>
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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/ga/2gak_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=2gak 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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2GAK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Beta-1,3-galactosyl-O-glycosyl-glycoprotein_beta-1,6-N-_acetylglucosaminyltransferase Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N- acetylglucosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.102 2.4.1.102] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GAK OCA].
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*[[O-GlcNAc transferase 3D structures|O-GlcNAc transferase 3D structures]]
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== References ==
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==Reference==
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<references/>
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X-ray crystal structure of leukocyte type core 2 beta1,6-N-acetylglucosaminyltransferase. Evidence for a convergence of metal ion-independent glycosyltransferase mechanism., Pak JE, Arnoux P, Zhou S, Sivarajah P, Satkunarajah M, Xing X, Rini JM, J Biol Chem. 2006 Sep 8;281(36):26693-701. Epub 2006 Jul 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16829524 16829524]
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__TOC__
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[[Category: Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N- acetylglucosaminyltransferase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Pak JE]]
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[[Category: Pak, J.E.]]
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[[Category: Rini JM]]
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[[Category: Rini, J.M.]]
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[[Category: NAG]]
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[[Category: cis-peptide]]
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[[Category: dimer]]
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[[Category: glycoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:04:54 2007''
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Current revision

X-ray crystal structure of murine leukocyte-type Core 2 b1,6-N-acetylglucosaminyltransferase (C2GnT-L)

PDB ID 2gak

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