1odh: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
==STRUCTURE OF THE GCM DOMAIN BOUND TO DNA==
 
<StructureSection load='1odh' size='340' side='right' caption='[[1odh]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
==Structure of the GCM domain bound to DNA==
<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 [http://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 [http://oca.weizmann.ac.il/oca-docs/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"><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='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=1odh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odh OCA], [http://pdbe.org/1odh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1odh RCSB], [http://www.ebi.ac.uk/pdbsum/1odh PDBsum]</span></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>
</table>
</table>
== Function ==
== Function ==
[[http://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]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/od/1odh_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/od/1odh_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata 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;">
<div style="background-color:#fffaf0;">
Line 31: Line 33:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Lk3 transgenic mice]]
[[Category: Large Structures]]
[[Category: Cohen, S X]]
[[Category: Mus musculus]]
[[Category: Muller, C W]]
[[Category: Cohen SX]]
[[Category: Dna-binding domain]]
[[Category: Muller CW]]
[[Category: Protein-dna complex]]
[[Category: Transcription factor]]
[[Category: Transcription factor-dna complex]]
[[Category: Transcription factor/dna]]

Latest revision as of 11:59, 9 May 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.

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[2]

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

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
  2. Cohen SX, Moulin M, Hashemolhosseini S, Kilian K, Wegner M, Muller CW. Structure of the GCM domain-DNA complex: a DNA-binding domain with a novel fold and mode of target site recognition. EMBO J. 2003 Apr 15;22(8):1835-45. PMID:12682016 doi:http://dx.doi.org/10.1093/emboj/cdg182

1odh, resolution 2.85Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA