2024-03-29T08:03:06Zhttps://eprints.lib.hokudai.ac.jp/dspace-oai/requestoai:eprints.lib.hokudai.ac.jp:2115/149182022-11-17T02:08:08Zhdl_2115_20055hdl_2115_8527Structure analysis of PH1161 protein, a transcriptional activator TenA homologue from the hyperthermophilic archaeon Pyrococcus horikoshiiItou, HiroshiYao, MinWatanabe, NobuhisaTanaka, Isaohaem oxygenase-1PH1161 proteinTenA proteintranscriptional activator464The crystal structure of the Bacillus subtilis TenA-homologue protein PH1161 from the hyperthermophilic archaebacterium Pyrococcus horikoshii was determined. TenA is known to belong to a new family of activators that stimulate the production of extracellular proteases in B. subtilis. A sequence-similarity search revealed that TenA-homologue proteins are widespread in bacteria and archaea, suggesting that this family of proteins plays an essential role in these organisms. In the present study, the first three-dimensional structure of a member of the TenA family of proteins was determined, unexpectedly revealing that the protein has a fold identical to that of haem oxygenase-1. Analysis has also shown that the protein has a unique ligand-binding pocket. Electron density of a bound ligand molecule was observed in this pocket. These results provide a valuable insight into the functional understanding of the TenA family of proteins.International Union of CrystallographyJournal Articleapplication/pdfhttp://hdl.handle.net/2115/14918https://eprints.lib.hokudai.ac.jp/dspace/bitstream/2115/14918/1/ACSD-BC60.pdf0907-4449Acta Crystallographica Section D Biological Crystallography606109411002004-06enginfo:pmid/15159569info:doi/10.1107/S0907444904008522publisher