Download MendeleyCrystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a variation of the RecA fold
Rossbach, M., Daumke, O., Klinger, C., Wittinghofer, A., Kaufmann, M.(2005) BMC Struct Biol 5: 7-7
- PubMed: 15777481
- DOI: https://doi.org/10.1186/1472-6807-5-7
- Primary Citation of Related Structures:
1YE8 - PubMed Abstract:
aaTHEP1, the gene product of aq_1292 from Aquifex aeolicus, shows sequence homology to proteins from most thermophiles, hyperthermophiles, and higher organisms such as man, mouse, and fly. In contrast, there are almost no homologous proteins in mesophilic unicellular microorganisms. aaTHEP1 is a thermophilic enzyme exhibiting both ATPase and GTPase activity in vitro. Although annotated as a nucleotide kinase, such an activity could not be confirmed for aaTHEP1 experimentally and the in vivo function of aaTHEP1 is still unknown.
Organizational Affiliation:
Institute of Neurobiochemistry, The Protein Chemistry Group, Witten/Herdecke University, Stockumer Strasse 10, 58448 Witten, Germany. miro@uni-wh.de
