1UDD
TenA homologue protein from P.horikoshii OT3
Summary for 1UDD
| Entry DOI | 10.2210/pdb1udd/pdb |
| Descriptor | transcriptional regulator (2 entities in total) |
| Functional Keywords | helix-bundle, lipid binding protein |
| Biological source | Pyrococcus horikoshii |
| Total number of polymer chains | 4 |
| Total formula weight | 106482.99 |
| Authors | Itou, H.,Yao, M.,Watanabe, N.,Tanaka, I. (deposition date: 2003-04-28, release date: 2004-06-01, Last modification date: 2023-12-27) |
| Primary citation | Itou, H.,Yao, M.,Watanabe, N.,Tanaka, I. Structure analysis of PH1161 protein, a transcriptional activator TenA homologue from the hyperthermophilic archaeon Pyrococcus horikoshii. Acta Crystallogr.,Sect.D, 60:1094-1100, 2004 Cited by PubMed Abstract: 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. PubMed: 15159569DOI: 10.1107/S0907444904008522 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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