This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1dch
From Proteopedia
(New page: 200px<br /><applet load="1dch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dch, resolution 3.0Å" /> '''CRYSTAL STRUCTURE OF ...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 14: | Line 14: | ||
[[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]] | ||
| Line 25: | Line 25: | ||
[[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
|
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 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
Page seeded by OCA on Thu Feb 21 12:15:12 2008
