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1foa

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[[Image:1foa.gif|left|200px]]<br /><applet load="1foa" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1foa, resolution 1.80&Aring;" />
 
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'''CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I==
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N:-acetylglucosaminyltransferase I (GnT I) serves as the gateway from oligomannose to hybrid and complex N:-glycans and plays a critical role in mammalian development and possibly all metazoans. We have determined the X-ray crystal structure of the catalytic fragment of GnT I in the absence and presence of bound UDP-GlcNAc/Mn(2+) at 1.5 and 1.8 A resolution, respectively. The structures identify residues critical for substrate binding and catalysis and provide evidence for similarity, at the mechanistic level, to the deglycosylation step of retaining beta-glycosidases. The structuring of a 13 residue loop, resulting from UDP-GlcNAc/Mn(2+) binding, provides an explanation for the ordered sequential 'Bi Bi' kinetics shown by GnT I. Analysis reveals a domain shared with Bacillus subtilis glycosyltransferase SpsA, bovine beta-1,4-galactosyl transferase 1 and Escherichia coli N:-acetylglucosamine-1-phosphate uridyltransferase. The low sequence identity, conserved fold and related functional features shown by this domain define a superfamily whose members probably share a common ancestor. Sequence analysis and protein threading show that the domain is represented in proteins from several glycosyltransferase families.
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<StructureSection load='1foa' size='340' side='right'caption='[[1foa]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1foa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FOA 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]] 1.8&#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>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UD1:URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE'>UD1</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=1foa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1foa OCA], [https://pdbe.org/1foa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1foa RCSB], [https://www.ebi.ac.uk/pdbsum/1foa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1foa ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MGAT1_RABIT MGAT1_RABIT] Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
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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/fo/1foa_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=1foa 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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1FOA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=UD1:'>UD1</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-1,3-mannosyl-glycoprotein_2-beta-N-acetylglucosaminyltransferase Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.101 2.4.1.101] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOA OCA].
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*[[O-GlcNAc transferase 3D structures|O-GlcNAc transferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily., Unligil UM, Zhou S, Yuwaraj S, Sarkar M, Schachter H, Rini JM, EMBO J. 2000 Oct 16;19(20):5269-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11032794 11032794]
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[[Category: Large Structures]]
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[[Category: Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase]]
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Single protein]]
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[[Category: Rini JM]]
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[[Category: Rini, J M.]]
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[[Category: Sarkar M]]
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[[Category: Sarkar, M.]]
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[[Category: Schachter H]]
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[[Category: Schachter, H.]]
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[[Category: Unligil UM]]
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[[Category: Unligil, U M.]]
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[[Category: Yuwaraj S]]
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[[Category: Yuwaraj, S.]]
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[[Category: Zhou S]]
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[[Category: Zhou, S.]]
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[[Category: GOL]]
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[[Category: MN]]
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[[Category: UD1]]
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[[Category: 2-n-acetylglucosaminyltransferase]]
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[[Category: 3-mannosyl-glycoprotein]]
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[[Category: alpha-1]]
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[[Category: beta-1]]
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[[Category: donor substrate and metal ion complex]]
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[[Category: n-acetylglucosaminyltransferase i]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:48 2008''
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Current revision

CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I

PDB ID 1foa

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