5TCE

N-terminal microdomain of 34-mers from HsDHODH - N-t(DH)

5TCE の概要

• エントリーDOI: 10.2210/pdb5tce/pdb
• NMR情報: BMRB: 30180
• 分子名称: Dihydroorotate dehydrogenase (quinone), mitochondrial (1 entity in total)
• 機能のキーワード: micelles, oxidoreductase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3831.32

構造登録者

Crusca, E.,Munte, C.E. (登録日: 2016-09-14, 公開日: 2017-09-20, 最終更新日: 2024-10-16)

主引用文献

Vicente, E.F.,Sahu, I.D.,Costa-Filho, A.J.,Cilli, E.M.,Lorigan, G.A.
Conformational changes of the HsDHODH N-terminal Microdomain via DEER Spectroscopy.
J Phys Chem B, 119:8693-8697, 2015

PubMed Abstract: The human enzyme dihydroorotate dehydrogenase (HsDHODH) has been studied for being a target for development of new antineoplasic and antiproliferative drugs. The synthetic peptide N-t(DH) represents the N-terminal microdomain of this enzyme, responsible for anchoring it to the inner mitochondrial membrane. Also, it is known to harbor quinones that are essential for enzyme catalysis. Here we report structural features of the peptide/membrane interactions obtained by using CD and DEER spectroscopic techniques, both in micelles and in lipid vesicles. The data revealed different peptide conformational states in micelles and liposomes, which could suggest that this microdomain acts in specific regions or areas of the mitochondria, which can be related with the control of the quinone access to the HsDHODH active site. This is the first study to report on conformational changes of the HsDHODH N-terminal microdomain through a combination of CD and DEER spectroscopic techniques.

PubMed: 26086954
DOI: 10.1021/acs.jpcb.5b01706

実験手法

SOLUTION NMR