4Q37

Crystal structure of the hypothetical protein TM0182 Thermotoga maritima, N-terminal domain.

4Q37 の概要

• エントリーDOI: 10.2210/pdb4q37/pdb
• 分子名称: Radical SAM protein, PLATINUM (II) ION (3 entities in total)
• 機能のキーワード: alpha-beta fold, unknown function
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 90259.34

構造登録者

Hocker, B.,Farias-Rico, J.A. (登録日: 2014-04-11, 公開日: 2014-07-16, 最終更新日: 2024-02-28)

主引用文献

Farias-Rico, J.A.,Schmidt, S.,Hocker, B.
Evolutionary relationship of two ancient protein superfolds.
Nat.Chem.Biol., 10:710-715, 2014

PubMed Abstract: Proteins are the molecular machines of the cell that fold into specific three-dimensional structures to fulfill their functions. To improve our understanding of how the structure and function of proteins arises, it is crucial to understand how evolution has generated the structural diversity we observe today. Classically, proteins that adopt different folds are considered to be nonhomologous. However, using state-of-the-art tools for homology detection, we found evidence of homology between proteins of two ancient and highly populated protein folds, the (βα)8-barrel and the flavodoxin-like fold. We detected a family of sequences that show intermediate features between both folds and determined what is to our knowledge the first representative crystal structure of one of its members, giving new insights into the evolutionary link of two of the earliest folds. Our findings contribute to an emergent vision where protein superfolds share common ancestry and encourage further approaches to complete the mapping of structure space onto sequence space.

PubMed: 25038785
DOI: 10.1038/nchembio.1579

実験手法

X-RAY DIFFRACTION (3.19 Å)