6P3L

Crystal Structure of Ketosteroid Isomerase from Mycobacterium hassiacum (mhKSI)

6P3L の概要

• エントリーDOI: 10.2210/pdb6p3l/pdb
• 分子名称: SnoaL-like domain protein, SULFATE ION, GUANIDINE, ... (4 entities in total)
• 機能のキーワード: isomerase, thermophile
• 由来する生物種: Mycobacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27698.74

構造登録者

Yabukarski, F.,Doukov, T.,Pinney, M.,Herschlag, D. (登録日: 2019-05-23, 公開日: 2020-05-27, 最終更新日: 2024-03-13)

主引用文献

Pinney, M.M.,Mokhtari, D.A.,Akiva, E.,Yabukarski, F.,Sanchez, D.M.,Liang, R.,Doukov, T.,Martinez, T.J.,Babbitt, P.C.,Herschlag, D.
Parallel molecular mechanisms for enzyme temperature adaptation.
Science, 371:-, 2021

PubMed Abstract: The mechanisms that underly the adaptation of enzyme activities and stabilities to temperature are fundamental to our understanding of molecular evolution and how enzymes work. Here, we investigate the molecular and evolutionary mechanisms of enzyme temperature adaption, combining deep mechanistic studies with comprehensive sequence analyses of thousands of enzymes. We show that temperature adaptation in ketosteroid isomerase (KSI) arises primarily from one residue change with limited, local epistasis, and we establish the underlying physical mechanisms. This residue change occurs in diverse KSI backgrounds, suggesting parallel adaptation to temperature. We identify residues associated with organismal growth temperature across 1005 diverse bacterial enzyme families, suggesting widespread parallel adaptation to temperature. We assess the residue properties, molecular interactions, and interaction networks that appear to underly temperature adaptation.

PubMed: 33674467
DOI: 10.1126/science.aay2784

実験手法

X-RAY DIFFRACTION (1.571 Å)