1odh: Difference between revisions

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<StructureSection load='1odh' size='340' side='right'caption='[[1odh]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='1odh' size='340' side='right'caption='[[1odh]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1odh]] is a 3 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=1ODH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ODH FirstGlance]. <br>
<table><tr><td colspan='2'>[[1odh]] is a 3 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=1ODH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ODH FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1odh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odh OCA], [https://pdbe.org/1odh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1odh RCSB], [https://www.ebi.ac.uk/pdbsum/1odh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1odh 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=1odh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odh OCA], [https://pdbe.org/1odh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1odh RCSB], [https://www.ebi.ac.uk/pdbsum/1odh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1odh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GCM1_MOUSE GCM1_MOUSE]] Transcription factor that is necessary for placental development (By similarity).<ref>PMID:8962155</ref>
[https://www.uniprot.org/uniprot/GCM1_MOUSE GCM1_MOUSE] Transcription factor that is necessary for placental development (By similarity).<ref>PMID:8962155</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1odh ConSurf].
</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=1odh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glia cell missing (GCM) transcription factors form a small family of transcriptional regulators in metazoans. The prototypical Drosophila GCM protein directs the differentiation of neuron precursor cells into glia cells, whereas mammalian GCM proteins are involved in placenta and parathyroid development. GCM proteins share a highly conserved 150 amino acid residue region responsible for DNA binding, known as the GCM domain. Here we present the crystal structure of the GCM domain from murine GCMa bound to its octameric DNA target site at 2.85 A resolution. The GCM domain exhibits a novel fold consisting of two domains tethered together by one of two structural Zn ions. We observe the novel use of a beta-sheet in DNA recognition, whereby a five- stranded beta-sheet protrudes into the major groove perpendicular to the DNA axis. The structure combined with mutational analysis of the target site and of DNA-contacting residues provides insight into DNA recognition by this new type of Zn-containing DNA-binding domain.
Structure of the GCM domain-DNA complex: a DNA-binding domain with a novel fold and mode of target site recognition.,Cohen SX, Moulin M, Hashemolhosseini S, Kilian K, Wegner M, Muller CW EMBO J. 2003 Apr 15;22(8):1835-45. PMID:12682016<ref>PMID:12682016</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1odh" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Cohen, S X]]
[[Category: Cohen SX]]
[[Category: Muller, C W]]
[[Category: Muller CW]]
[[Category: Dna-binding domain]]
[[Category: Protein-dna complex]]
[[Category: Transcription factor]]
[[Category: Transcription factor-dna complex]]
[[Category: Transcription factor/dna]]

Revision as of 08:46, 17 April 2024

Structure of the GCM domain bound to DNAStructure of the GCM domain bound to DNA

Structural highlights

1odh is a 3 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 2.85Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GCM1_MOUSE Transcription factor that is necessary for placental development (By similarity).[1]

Evolutionary Conservation

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

References

  1. ↑ Akiyama Y, Hosoya T, Poole AM, Hotta Y. The gcm-motif: a novel DNA-binding motif conserved in Drosophila and mammals. Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14912-6. PMID:8962155

1odh, resolution 2.85Å

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