5eog

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==Structure of full-length human MAB21L1==
==Structure of full-length human MAB21L1==
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<StructureSection load='5eog' size='340' side='right' caption='[[5eog]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
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<StructureSection load='5eog' size='340' side='right'caption='[[5eog]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5eog]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EOG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5eog]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EOG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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]] 3.05&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5eog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eog OCA], [http://pdbe.org/5eog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eog RCSB], [http://www.ebi.ac.uk/pdbsum/5eog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eog ProSAT]</span></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=CIT:CITRIC+ACID'>CIT</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=5eog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eog OCA], [https://pdbe.org/5eog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eog RCSB], [https://www.ebi.ac.uk/pdbsum/5eog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eog ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MB211_HUMAN MB211_HUMAN]] Required for several aspects of embryonic development including normal development of the eye.
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[https://www.uniprot.org/uniprot/MB211_HUMAN MB211_HUMAN] Required for several aspects of embryonic development including normal development of the eye.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The exceptionally conserved metazoan MAB21 proteins are implicated in cell fate decisions and share considerable sequence homology with the cyclic GMP-AMP synthase. cGAS is the major innate immune sensor for cytosolic DNA and produces the second messenger 2'-5', 3'-5' cyclic GMP-AMP. Little is known about the structure and biochemical function of other proteins of the cGAS-MAB21 subfamily, such as MAB21L1, MAB21L2 and MAB21L3. We have determined the crystal structure of human full-length MAB21L1. Our analysis reveals high structural conservation between MAB21L1 and cGAS but also uncovers important differences. Although monomeric in solution, MAB21L1 forms a highly symmetric double-pentameric oligomer in the crystal, raising the possibility that oligomerization could be a feature of MAB21L1. In the crystal, MAB21L1 is in an inactive conformation requiring a conformational change - similar to cGAS - to develop any nucleotidyltransferase activity. Co-crystallization with NTP identified a putative ligand binding site of MAB21 proteins that corresponds to the DNA binding site of cGAS. Finally, we offer a structure-based explanation for the effects of MAB21L2 mutations in patients with eye malformations. The underlying residues participate in fold-stabilizing interaction networks and mutations destabilize the protein. In summary, we provide a first structural framework for MAB21 proteins.
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Structural and biochemical characterization of the cell fate determining nucleotidyltransferase fold protein MAB21L1.,de Oliveira Mann CC, Kiefersauer R, Witte G, Hopfner KP Sci Rep. 2016 Jun 8;6:27498. doi: 10.1038/srep27498. PMID:27271801<ref>PMID:27271801</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 5eog" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hopfner, K P]]
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[[Category: Homo sapiens]]
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[[Category: Mann, C C.de Oliveira]]
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[[Category: Large Structures]]
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[[Category: Witte, G]]
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[[Category: Hopfner K-P]]
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[[Category: Nucleotidyltransferase fold protein]]
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[[Category: Witte G]]
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[[Category: Transferase]]
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[[Category: De Oliveira Mann CC]]

Current revision

Structure of full-length human MAB21L1

PDB ID 5eog

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