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[[Image:2j0a.jpg|left|200px]]


{{Structure
==Structure of the catalytic domain of mouse Manic Fringe==
|PDB= 2j0a |SIZE=350|CAPTION= <scene name='initialview01'>2j0a</scene>, resolution 1.80&Aring;
<StructureSection load='2j0a' size='340' side='right'caption='[[2j0a]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:K+Binding+Site+For+Chain+A'>AC1</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=K:POTASSIUM ION'>K</scene>
<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>
|ACTIVITY= [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]  
</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>
|GENE=  
<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>
}}
<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>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j0/2j0a_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''STRUCTURE OF THE CATALYTIC DOMAIN OF MOUSE MANIC FRINGE'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2j0a" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[O-GlcNAc transferase 3D structures|O-GlcNAc transferase 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase]]
[[Category: Chen Y-W]]
[[Category: Single protein]]
[[Category: Clausen H]]
[[Category: Chen, Y W.]]
[[Category: Cohen SM]]
[[Category: Clausen, H.]]
[[Category: Conti E]]
[[Category: Cohen, S M.]]
[[Category: Jinek M]]
[[Category: Conti, E.]]
[[Category: Jinek, M.]]
[[Category: K]]
[[Category: SO4]]
[[Category: developmental protein]]
[[Category: glycoprotein]]
[[Category: glycosyltransferase]]
[[Category: golgi apparatus]]
[[Category: membrane]]
[[Category: notch signaling]]
[[Category: signal-anchor]]
[[Category: transferase]]
[[Category: transmembrane]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:35:49 2008''

Latest revision as of 04:05, 21 November 2024

Structure of the catalytic domain of mouse Manic FringeStructure of the catalytic domain of mouse Manic Fringe

Structural highlights

2j0a is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Jinek M, Chen YW, Clausen H, Cohen SM, Conti E. Structural insights into the Notch-modifying glycosyltransferase Fringe. Nat Struct Mol Biol. 2006 Oct;13(10):945-6. Epub 2006 Sep 10. PMID:16964258 doi:10.1038/nsmb1144

2j0a, resolution 1.80Å

Drag the structure with the mouse to rotate

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