1tq5

Crystal Structure of YhhW from Escherichia coli

spinqualitylabelsall models 1tq5, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tq5 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.76Å Ligands: CD, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function YHHW_ECOLI Has quercetin 2,3-dioxygenase activity in vitro. Its physiological role is unknown; however, may provide a mechanism that would avoid inhibition of key cellular proteins, such as DNA gyrase, by quercetin. 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 Pirin is a recently identified eukaryotic protein implicated in transcriptional activation and apoptosis. Homologues of Pirin are highly conserved in both prokaryotes and eukaryotes, but their function remains poorly understood. We present here the crystal structure of the yhhW gene product, a putative Pirin homologue, from Escherichia coli and confirm its structural similarity to Pirin. The YhhW protein displays a bicupin fold with a single N-terminal metal coordination site. Molecular surface comparisons of YhhW and Pirin with structurally similar proteins suggested quercetin as a potential ligand. We demonstrate that both bacterial and human Pirins have quercetinase activity, which is inhibited by the addition of typical inhibitors of the quercetin 2,3-dioxygenase reaction. We also demonstrate the release of carbon monoxide as a reaction product. This is the first report of enzymatic activity for any member of the Pirin family and may be an important connection to their roles in transcriptional regulation. Structural and biochemical analysis reveal pirins to possess quercetinase activity.,Adams M, Jia Z J Biol Chem. 2005 Aug 5;280(31):28675-82. Epub 2005 Jun 11. PMID:15951572 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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