1dcp | pdb_00001dcp

DCOH, A BIFUNCTIONAL PROTEIN-BINDING TRANSCRIPTIONAL COACTIVATOR, COMPLEXED WITH BIOPTERIN

spinqualitylabelsall models 1dcp, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dcp is a 8 chain structure with sequence from Buffalo rat. The August 2015 RCSB PDB Molecule of the Month feature on Tetrahydrobiopterin Biosynthesis by David Goodsell is 10.2210/rcsb_pdb/mom_2015_8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HBI Activity: 4a-hydroxytetrahydrobiopterin dehydratase, with EC number 4.2.1.96 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed DCoH, the dimerization cofactor of hepatocyte nuclear factor 1 (HNF-1), functions as both a transcriptional coactivator and a pterin dehydratase. To probe the relationship between these two functions, the X-ray crystal structures of the free enzyme and its complex with the product analogue 7,8-dihydrobiopterin were refined at 2.3 A resolution. The ligand binds at four sites per tetrameric enzyme, with little apparent conformational change in the protein. Each active-site cleft is located in a subunit interface, adjacent to a prominent saddle motif that has structural similarities to the TATA binding protein. The pterin binds within an arch of aromatic residues that extends across one dimer interface. The bound ligand makes contacts to three conserved histidines, and this arrangement restricts proposals for the enzymatic mechanism of dehydration. The dihedral symmetry of DCoH suggests that binding to the dimerization domain of HNF-1 likely involves the superposition of two-fold rotation axes of the two proteins. High-resolution structures of the bifunctional enzyme and transcriptional coactivator DCoH and its complex with a product analogue.,Cronk JD, Endrizzi JA, Alber T Protein Sci. 1996 Oct;5(10):1963-72. PMID:8897596 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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