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New page: left|200px<br /><applet load="1dch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dch, resolution 3.0Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1dch.gif|left|200px]]<br /><applet load="1dch" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dch, resolution 3.0&Aring;" />
'''CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR'''<br />


==Overview==
==CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR==
DCoH, the dimerization cofactor of hepatocyte nuclear factor-1, stimulates, gene expression by associating with specific DNA binding proteins and also, catalyzes the dehydration of the biopterin cofactor of phenylalanine, hydroxylase. The x-ray crystal structure determined at 3 angstrom, resolution reveals that DCoH forms a tetramer containing two saddle-shaped, grooves that comprise likely macromolecule binding sites. Two equivalent, enzyme active sites flank each saddle, suggesting that there is a spatial, connection between the catalytic and binding activities. Structural, similarities between the DCoH fold and nucleic acid-binding proteins argue, that the saddle motif has evolved to bind diverse ligands or that DCoH, unexpectedly may bind nucleic acids.
<StructureSection load='1dch' size='340' side='right'caption='[[1dch]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1dch]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCH FirstGlance]. <br>
1DCH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DCH OCA].  
</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&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dch OCA], [https://pdbe.org/1dch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dch RCSB], [https://www.ebi.ac.uk/pdbsum/1dch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dch ProSAT]</span></td></tr>
Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator., Endrizzi JA, Cronk JD, Wang W, Crabtree GR, Alber T, Science. 1995 Apr 28;268(5210):556-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7725101 7725101]
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHS_RAT PHS_RAT] Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity.<ref>PMID:1763325</ref> <ref>PMID:8444860</ref>
== 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/dc/1dch_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1dch ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Alber T]]
[[Category: Alber, T.]]
[[Category: Crabtree GR]]
[[Category: Crabtree, G.R.]]
[[Category: Cronk JD]]
[[Category: Cronk, J.D.]]
[[Category: Endrizzi JA]]
[[Category: Endrizzi, J.A.]]
[[Category: Wang W]]
[[Category: Wang, W.]]
[[Category: SO4]]
[[Category: 4a-carbinolamine dehydratase]]
[[Category: dehydratase]]
[[Category: dimerization cofactor]]
[[Category: transcriptional simulator]]
[[Category: transregulator of homeodomain proteins]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:10:11 2007''
Retrieved from "https://proteopedia.org/1dch"