1YE8
Crystal Structure of THEP1 from the hyperthermophile Aquifex aeolicus
Summary for 1YE8
| Entry DOI | 10.2210/pdb1ye8/pdb |
| Descriptor | Hypothetical UPF0334 kinase-like protein AQ_1292, MAGNESIUM ION, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | mixed alpha-beta protein; rossmann fold, signaling protein, transferase |
| Biological source | Aquifex aeolicus |
| Total number of polymer chains | 1 |
| Total formula weight | 20899.32 |
| Authors | Rossbach, M.,Daumke, O.,Klinger, C.,Wittinghofer, A.,Kaufmann, M. (deposition date: 2004-12-28, release date: 2005-03-29, Last modification date: 2024-11-13) |
| Primary citation | Rossbach, M.,Daumke, O.,Klinger, C.,Wittinghofer, A.,Kaufmann, M. Crystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a variation of the RecA fold BMC Struct.Biol., 5:7-7, 2005 Cited by 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. PubMed: 15777481DOI: 10.1186/1472-6807-5-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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