5NE7

Crystal structure of H60A mutant of Thermotoga maritima TmPEP1050 aminopeptidase

5NE7 の概要

• エントリーDOI: 10.2210/pdb5ne7/pdb
• 分子名称: AMINOPEPTIDASE, CITRIC ACID (3 entities in total)
• 機能のキーワード: aminopeptidase, m42 family, tetrahedral structure, metal ion binding, lyase
• 由来する生物種: Thermotoga maritima MSB8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72278.58

構造登録者

Dutoit, R. (登録日: 2017-03-10, 公開日: 2018-05-16, 最終更新日: 2024-01-17)

主引用文献

Dutoit, R.,Van Gompel, T.,Brandt, N.,Van Elder, D.,Van Dyck, J.,Sobott, F.,Droogmans, L.
How metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 ofThermotoga maritima.
J.Biol.Chem., 294:17777-17789, 2019

PubMed Abstract: The M42 aminopeptidases are dinuclear aminopeptidases displaying a peculiar tetrahedron-shaped structure with 12 subunits. Their quaternary structure results from the self-assembly of six dimers controlled by their divalent metal ion cofactors. The oligomeric-state transition remains debated despite the structural characterization of several archaeal M42 aminopeptidases. The main bottleneck is the lack of dimer structures, hindering the understanding of structural changes occurring during the oligomerization process. We present the first dimer structure of an M42 aminopeptidase, TmPep1050 of , along with the dodecamer structure. The comparison of both structures has allowed us to describe how the metal ion cofactors modulate the active-site fold and, subsequently, affect the interaction interface between dimers. A mutational study shows that the M1 site strictly controls dodecamer formation. The dodecamer structure of TmPep1050 also reveals that a part of the dimerization domain delimits the catalytic pocket and could participate in substrate binding.

PubMed: 31611236
DOI: 10.1074/jbc.RA119.009281

実験手法

X-RAY DIFFRACTION (1.84 Å)