5Y0M

Structure of 6-aminohexanoate-oligomer hydrolase from Arthrobacter sp. KI72., D36A/D122G/H130Y/E263Q mutant

5Y0M の概要

• エントリーDOI: 10.2210/pdb5y0m/pdb
• 分子名称: Endo-type 6-aminohexanoate oligomer hydrolase, GLYCEROL, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: nylon oligomer, hydrolase
• 由来する生物種: Flavobacterium sp. KI723T1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75159.35

構造登録者

Negoro, S.,Shibata, N.,Nagai, K.,Higuchi, Y. (登録日: 2017-07-18, 公開日: 2018-07-25, 最終更新日: 2023-11-15)

主引用文献

Negoro, S.,Shibata, N.,Lee, Y.H.,Takehara, I.,Kinugasa, R.,Nagai, K.,Tanaka, Y.,Kato, D.I.,Takeo, M.,Goto, Y.,Higuchi, Y.
Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolase
Sci Rep, 8:9725-9725, 2018

PubMed Abstract: Nylon hydrolase (NylC) is initially expressed as an inactive precursor (36 kDa). The precursor is cleaved autocatalytically at Asn266/Thr267 to generate an active enzyme composed of an α subunit (27 kDa) and a β subunit (9 kDa). Four αβ heterodimers (molecules A-D) form a doughnut-shaped quaternary structure. In this study, the thermostability of the parental NylC was altered by amino acid substitutions located at the A/D interface (D122G/H130Y/D36A/L137A) or the A/B interface (E263Q) and spanned a range of 47 °C. Considering structural, biophysical, and biochemical analyses, we discuss the structural basis of the stability of nylon hydrolase. From the analytical centrifugation data obtained regarding the various mutant enzymes, we conclude that the assembly of the monomeric units is dynamically altered by the mutations. Finally, we propose a model that can predict whether the fate of the nascent polypeptide will be correct subunit assembly, inappropriate protein-protein interactions causing aggregation, or intracellular degradation of the polypeptide.

PubMed: 29950566
DOI: 10.1038/s41598-018-27860-w

実験手法

X-RAY DIFFRACTION (1.03 Å)