Structure analysis of PH1161 protein, a transcriptional activator TenA homologue from the hyperthermophilic archaeon Pyrococcus horikoshii
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概要
- 論文の詳細を見る
The 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 Crystallographyの論文
著者
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Yao Min
Faculty Of Adv. Life Sci. Hokkaido Univ.
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Watanabe Nobuhisa
Faculty Of Adv. Life Sci. Hokkaido Univ.
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Tanaka Isao
Graduate School Of Life Science Hokkaido University
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Yao Min
Graduate School Of Life Science Hokkaido University
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