2qcx

Crystal structure of Bacillus subtilis TenA Y112F mutant complexed with formyl aminomethyl pyrimidine

spinqualitylabelsall models 2qcx, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2qcx is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: PF1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TENA_BACSU Stimulates the production of several extracellular degradative enzymes at the transcriptional level, probably by interfering with DegS and DegU, which are required for this effect. Is not an essential protein, but affects the sporulation frequency. 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 TenA catalyzes the hydrolysis of 4-amino-5-aminomethyl-2-methylpyrimidine and participates in the salvage of base-degraded thiamin. Here, we describe mutagenesis of the active site of TenA guided by structures of the enzyme complexed to a substrate analog and to the product. Catalytic roles for each of the active site residues are identified and a mechanism for the reaction is described. Mutagenesis studies on TenA: a thiamin salvage enzyme from Bacillus subtilis.,Jenkins AL, Zhang Y, Ealick SE, Begley TP Bioorg Chem. 2008 Feb;36(1):29-32. Epub 2007 Dec 3. PMID:18054064 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thiaminase Transcriptional activator 3D structures

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