1dch
From Proteopedia
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|PDB= 1dch |SIZE=350|CAPTION= <scene name='initialview01'>1dch</scene>, resolution 3.0Å | |PDB= 1dch |SIZE=350|CAPTION= <scene name='initialview01'>1dch</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dch OCA], [http://www.ebi.ac.uk/pdbsum/1dch PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dch RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Endrizzi, J A.]] | [[Category: Endrizzi, J A.]] | ||
[[Category: Wang, W.]] | [[Category: Wang, W.]] | ||
| - | [[Category: SO4]] | ||
[[Category: 4a-carbinolamine dehydratase]] | [[Category: 4a-carbinolamine dehydratase]] | ||
[[Category: dehydratase]] | [[Category: dehydratase]] | ||
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[[Category: transregulator of homeodomain protein]] | [[Category: transregulator of homeodomain protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:38:53 2008'' |
Revision as of 16:38, 30 March 2008
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| , resolution 3.0Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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