1dch: Difference between revisions
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=" | [[Image:1dch.gif|left|200px]]<br /><applet load="1dch" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1dch, resolution 3.0Å" /> | caption="1dch, resolution 3.0Å" /> | ||
'''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 | 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:// | 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 | [[Category: Crabtree, G R.]] | ||
[[Category: Cronk, J | [[Category: Cronk, J D.]] | ||
[[Category: Endrizzi, J | [[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:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:12 2008'' | ||
Revision as of 10:15, 21 February 2008
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CRYSTAL STRUCTURE OF DCOH, A BIFUNCTIONAL, PROTEIN-BINDING TRANSCRIPTION COACTIVATOR
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.
About this Structure
1DCH is a Single protein structure of sequence from Rattus norvegicus with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
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:7725101
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