1YE8

Crystal Structure of THEP1 from the hyperthermophile Aquifex aeolicus

1YE8 の概要

• エントリーDOI: 10.2210/pdb1ye8/pdb
• 分子名称: Hypothetical UPF0334 kinase-like protein AQ_1292, MAGNESIUM ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: mixed alpha-beta protein; rossmann fold, signaling protein, transferase
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20899.32

構造登録者

Rossbach, M.,Daumke, O.,Klinger, C.,Wittinghofer, A.,Kaufmann, M. (登録日: 2004-12-28, 公開日: 2005-03-29, 最終更新日: 2024-11-13)

主引用文献

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

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: 15777481
DOI: 10.1186/1472-6807-5-7

実験手法

X-RAY DIFFRACTION (1.4 Å)