2j0a

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[[Image:2j0a.jpg|left|200px]]
 
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{{Structure
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==Structure of the catalytic domain of mouse Manic Fringe==
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|PDB= 2j0a |SIZE=350|CAPTION= <scene name='initialview01'>2j0a</scene>, resolution 1.80&Aring;
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<StructureSection load='2j0a' size='340' side='right'caption='[[2j0a]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:K+Binding+Site+For+Chain+A'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[2j0a]] is a 1 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=2J0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J0A FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/O-fucosylpeptide_3-beta-N-acetylglucosaminyltransferase O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.222 2.4.1.222] </span>
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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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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=2j0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j0a OCA], [https://pdbe.org/2j0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j0a RCSB], [https://www.ebi.ac.uk/pdbsum/2j0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j0a ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j0a OCA], [http://www.ebi.ac.uk/pdbsum/2j0a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j0a RCSB]</span>
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== Evolutionary Conservation ==
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}}
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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/j0/2j0a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2j0a ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fringe proteins are beta1,3-N-acetylglucosaminyltransferases that modify Notch receptors, altering their ligand-binding specificity to regulate Notch signaling in development. We present the crystal structure of mouse Manic Fringe bound to UDP and manganese. The structure reveals amino acid residues involved in recognition of donor substrates and catalysis, and a putative binding pocket for acceptor substrates. Mutations of several invariant residues in this pocket impair Fringe activity in vivo.
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'''STRUCTURE OF THE CATALYTIC DOMAIN OF MOUSE MANIC FRINGE'''
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Structural insights into the Notch-modifying glycosyltransferase Fringe.,Jinek M, Chen YW, Clausen H, Cohen SM, Conti E Nat Struct Mol Biol. 2006 Oct;13(10):945-6. Epub 2006 Sep 10. PMID:16964258<ref>PMID:16964258</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2j0a" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Fringe proteins are beta1,3-N-acetylglucosaminyltransferases that modify Notch receptors, altering their ligand-binding specificity to regulate Notch signaling in development. We present the crystal structure of mouse Manic Fringe bound to UDP and manganese. The structure reveals amino acid residues involved in recognition of donor substrates and catalysis, and a putative binding pocket for acceptor substrates. Mutations of several invariant residues in this pocket impair Fringe activity in vivo.
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*[[O-GlcNAc transferase 3D structures|O-GlcNAc transferase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2J0A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J0A OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Structural insights into the Notch-modifying glycosyltransferase Fringe., Jinek M, Chen YW, Clausen H, Cohen SM, Conti E, Nat Struct Mol Biol. 2006 Oct;13(10):945-6. Epub 2006 Sep 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16964258 16964258]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase]]
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[[Category: Chen Y-W]]
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[[Category: Single protein]]
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[[Category: Clausen H]]
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[[Category: Chen, Y W.]]
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[[Category: Cohen SM]]
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[[Category: Clausen, H.]]
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[[Category: Conti E]]
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[[Category: Cohen, S M.]]
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[[Category: Jinek M]]
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[[Category: Conti, E.]]
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[[Category: Jinek, M.]]
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[[Category: developmental protein]]
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[[Category: glycoprotein]]
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[[Category: glycosyltransferase]]
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[[Category: golgi apparatus]]
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[[Category: membrane]]
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[[Category: notch signaling]]
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[[Category: signal-anchor]]
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[[Category: transferase]]
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[[Category: transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:51:16 2008''
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Current revision

Structure of the catalytic domain of mouse Manic Fringe

PDB ID 2j0a

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