1dch: Difference between revisions

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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"  
[[Image:1dch.gif|left|200px]]<br /><applet load="1dch" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dch, resolution 3.0&Aring;" />
caption="1dch, resolution 3.0&Aring;" />
'''CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR'''<br />
'''CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
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].  
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 <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCH OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Alber, T.]]
[[Category: Alber, T.]]
[[Category: Crabtree, G.R.]]
[[Category: Crabtree, G R.]]
[[Category: Cronk, J.D.]]
[[Category: Cronk, J D.]]
[[Category: Endrizzi, J.A.]]
[[Category: Endrizzi, J A.]]
[[Category: Wang, W.]]
[[Category: Wang, W.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: transregulator of homeodomain proteins]]
[[Category: transregulator of homeodomain proteins]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:10:11 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:12 2008''