5IMA

Xanthomonas campestris Peroxiredoxin Q - Structure F2

5IMA の概要

• エントリーDOI: 10.2210/pdb5ima/pdb
• 関連するPDBエントリー: 3gkk 3gkm 3gkn 5IIZ 5IM9 5IMC 5IMD 5IMF 5IMV 5IMZ
• 分子名称: Bacterioferritin comigratory protein, SODIUM ION, FORMIC ACID, ... (4 entities in total)
• 機能のキーワード: prxq, bcp, peroxidase, redox, oxidoreductase
• 由来する生物種: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17325.60

構造登録者

Perkins, A.,Parsonage, D.,Nelson, K.J.,Poole, L.B.,Karplus, A. (登録日: 2016-03-06, 公開日: 2016-09-21, 最終更新日: 2024-10-23)

主引用文献

Perkins, A.,Parsonage, D.,Nelson, K.J.,Ogba, O.M.,Cheong, P.H.,Poole, L.B.,Karplus, P.A.
Peroxiredoxin Catalysis at Atomic Resolution.
Structure, 24:1668-1678, 2016

PubMed Abstract: Peroxiredoxins (Prxs) are ubiquitous cysteine-based peroxidases that guard cells against oxidative damage, are virulence factors for pathogens, and are involved in eukaryotic redox regulatory pathways. We have analyzed catalytically active crystals to capture atomic resolution snapshots of a PrxQ subfamily enzyme (from Xanthomonas campestris) proceeding through thiolate, sulfenate, and sulfinate species. These analyses provide structures of unprecedented accuracy for seeding theoretical studies, and reveal conformational intermediates giving insight into the reaction pathway. Based on a highly non-standard geometry seen for the sulfenate intermediate, we infer that the sulfenate formation itself can strongly promote local unfolding of the active site to enhance productive catalysis. Further, these structures reveal that preventing local unfolding, in this case via crystal contacts, results in facile hyperoxidative inactivation even for Prxs normally resistant to such inactivation. This supports previous proposals that conformation-specific inhibitors may be useful for achieving selective inhibition of Prxs that are drug targets.

PubMed: 27594682
DOI: 10.1016/j.str.2016.07.012

実験手法

X-RAY DIFFRACTION (1.04 Å)