| Primary Identifier | IPR002767 | Type | Domain |
| Short Name | Thiamine_BP |
| description | The crystal structure of two of these members shows that this domain has a ferredoxin like fold and is likely to exists as at least homodimers. Sulphate ions are located at the dimer interfaces, which are thought to confer additional stability. Although the function of this domain remains to be identified, its structure suggests a role in protein-protein interactions possibly regulated by the binding of small-molecule ligands []. Solution of the structure of the hyperthermophilic anaerobic Thermotoga maritima sequence, (), shows that this has a beta-α-β-beta-α-β ferredoxin-like fold and assembles as a homotetramer. It was possible to identify a pocket in each monomer that bound an unidentified ligand. It was also found that it bound charged thiamine though not hydroxymethyl pyrimidine. Under oxidative conditions this bacterium is under stress, and the transcriptional unit within which this protein is expressed is up-regulated in these conditions, suggesting that the chelation of cytoplasmic thaimine is part of the response mechanism to such oxidatvie stress, which is mediated by this family []. |
