Crystal structure of THEP1 from the hyperthermophile <Emphasis Type="Italic">Aquifex aeolicus</Emphasis>: a variation of the RecA fold |
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| Authors: | Michael?Ro?bach Oliver?Daumke Claudia?Klinger Alfred?Wittinghofer Email author" target="_blank">Michael?KaufmannEmail author |
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| Institution: | (1) Institute of Neurobiochemistry, The Protein Chemistry Group, Witten/Herdecke University, Stockumer Strasse 10, 58448 Witten, Germany;(2) Max Planck Institute of Molecular Physiology, Department of Structural Biology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany |
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| Abstract: | Background 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. |
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