3qh2 | pdb_00003qh2

Crystal structure of TenI from Bacillus subtilis complexed with product cThz-P

spinqualitylabelsall models 3qh2, resolution 2.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qh2 is a 4 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3NM, SO4 Gene: tenI, BSU11660 ("Vibrio subtilis" Ehrenberg 1835) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TENI_BACSU] Reduces the stimulatory effect of the TenA transcriptional activator on production of certain extracellular enzymes. Is not an essential protein, but affects the sporulation frequency. Publication Abstract from PubMed In many bacteria tenI is found clustered with genes involved in thiamin thiazole biosynthesis. However, while TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity and the role of this enzyme in thiamin biosynthesis remains unknown. In this paper, we identify the function of TenI as a thiazole tautomerase, describe the structure of the enzyme complexed with its reaction product, identify the substrate phosphate and histidine 122 as the acid/base residues involved in catalysis and propose a mechanism for the reaction. The identification of the function of TenI completes the identification of all of the enzymes needed for thiamin biosynthesis by the major bacterial pathway. A Missing Enzyme in Thiamin Thiazole Biosynthesis: Identification of TenI as a Thiazole Tautomerase.,Hazra AB, Han Y, Chatterjee A, Zhang Y, Lai RY, Ealick SE, Begley TP J Am Chem Soc. 2011 May 2. PMID:21534620 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA