7EPS

Partial Consensus L-threonine 3-dehydrogenase (E-change)

7EPS の概要

• エントリーDOI: 10.2210/pdb7eps/pdb
• 分子名称: L-threonine 3-dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, THREONINE, ... (5 entities in total)
• 機能のキーワード: l-threonine 3-dehydrogenase, artificial protein, oxidoreductase
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 151117.75

構造登録者

Kozuka, K.,Nakano, S.,Asano, Y.,Ito, S. (登録日: 2021-04-27, 公開日: 2021-08-11, 最終更新日: 2023-11-29)

主引用文献

Kozuka, K.,Nakano, S.,Asano, Y.,Ito, S.
Partial Consensus Design and Enhancement of Protein Function by Secondary-Structure-Guided Consensus Mutations.
Biochemistry, 60:2309-2319, 2021

PubMed Abstract: Consensus design (CD) is a representative sequence-based protein design method that enables the design of highly functional proteins by analyzing vast amounts of protein sequence data. This study proposes a partial consensus design (PCD) of a protein as a derivative approach of CD. The method replaces the target protein sequence with a consensus sequence in a secondary-structure-dependent manner (i.e., regionally dependent and divided into α-helix, β-sheet, and loop regions). In this study, we generated several artificial partial consensus l-threonine 3-dehydrogenases (PcTDHs) by PCD using the TDH from (CnTDH) as a target protein. Structural and functional analysis of PcTDHs suggested that thermostability would be independently improved when consensus mutations are introduced into the loop region of TDHs. On the other hand, enzyme kinetic parameters (/) and average productivity would be synergistically enhanced by changing the combination of the mutations-replacement of one region of CnTDH with a consensus sequence provided only negative effects, but the negative effects were nullified when the two regions were replaced simultaneously. Taken together, we propose the hypothesis that there are protein regions that encode individual protein properties, such as thermostability and activity, and that the introduction of consensus mutations into these regions could additively or synergistically modify their functions.

PubMed: 34254784
DOI: 10.1021/acs.biochem.1c00309

実験手法

X-RAY DIFFRACTION (2.102 Å)