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3mlo

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Current revision (08:48, 7 February 2024) (edit) (undo)
 
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<StructureSection load='3mlo' size='340' side='right'caption='[[3mlo]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
<StructureSection load='3mlo' size='340' side='right'caption='[[3mlo]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3mlo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3mlo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 3.01&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3mln|3mln]], [[3mlp|3mlp]]</div></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=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ebf1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3mlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlo OCA], [https://pdbe.org/3mlo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlo RCSB], [https://www.ebi.ac.uk/pdbsum/3mlo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlo ProSAT]</span></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=3mlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlo OCA], [https://pdbe.org/3mlo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlo RCSB], [https://www.ebi.ac.uk/pdbsum/3mlo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/COE1_MOUSE COE1_MOUSE]] Transcriptional activator which recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'.<ref>PMID:20876732</ref>
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[https://www.uniprot.org/uniprot/COE1_MOUSE COE1_MOUSE] Transcriptional activator which recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'.<ref>PMID:20876732</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Early B-cell factor 1 (Ebf1) is a key transcriptional determinant of B-lymphocyte differentiation whose DNA-binding domain has no sequence similarity to other transcription factor families. Here we report the crystal structure of an Ebf1 dimer bound to its palindromic recognition site. The DNA-binding domain adopts a pseudoimmunoglobulin-like fold with novel topology, but is structurally similar to the Rel homology domains of NFAT and NF-kappaB. Ebf1 contacts the DNA with two loop-based modules and a unique Zn coordination motif whereby each Ebf1 monomer interacts with both palindromic half-sites. This unusual mode of DNA recognition generates an extended contact area that may be crucial for the function of Ebf1 in chromatin.
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Structure of an Ebf1:DNA complex reveals unusual DNA recognition and structural homology with Rel proteins.,Treiber N, Treiber T, Zocher G, Grosschedl R Genes Dev. 2010 Oct 15;24(20):2270-5. Epub 2010 Sep 28. PMID:20876732<ref>PMID:20876732</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 3mlo" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Grosschedl, R]]
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[[Category: Synthetic construct]]
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[[Category: Treiber, N]]
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[[Category: Grosschedl R]]
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[[Category: Treiber, T]]
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[[Category: Treiber N]]
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[[Category: Zocher, G]]
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[[Category: Treiber T]]
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[[Category: Dna]]
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[[Category: Zocher G]]
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[[Category: Ebf]]
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[[Category: Ebf-1]]
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[[Category: Pseudo-ig-fold]]
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[[Category: Transcription factor]]
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[[Category: Transcription-dna complex]]
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[[Category: Zn-finger]]
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[[Category: Zn-knuckle]]
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Current revision

DNA binding domain of Early B-cell Factor 1 (Ebf1) bound to DNA (Crystal form I)

PDB ID 3mlo

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