5FNN

Iron and Selenomethionine containing Iron sulfur cluster repair protein YtfE

5FNN の概要

• エントリーDOI: 10.2210/pdb5fnn/pdb
• 関連するPDBエントリー: 5FNP 5FNY
• 分子名称: IRON-SULFUR CLUSTER REPAIR PROTEIN YTFE, FE (II) ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, nitric oxide, iron-sulfur cluster repair, di-fe center.
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cytoplasm : P69506
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51061.00

構造登録者

Lo, F.-C.,Hsieh, C.-C.,Maestre-Reyna, M.,Chen, C.-Y.,Ko, T.-P.,Horng, Y.-C.,Lai, Y.-C.,Chiang, Y.-W.,Chou, C.-M.,Chiang, C.-H.,Huang, W.-N.,Liaw, W.-F. (登録日: 2015-11-16, 公開日: 2016-04-27, 最終更新日: 2024-11-06)

主引用文献

Lo, F.-C.,Hsieh, C.-C.,Maestre-Reyna, M.,Chen, C.-Y.,Ko, T.-P.,Horng, Y.-C.,Lai, Y.-C.,Chiang, Y.-W.,Chou, C.-M.,Chiang, C.-H.,Huang, W.-N.,Liaw, W.-F.
Crystal Structure of the Repair of Iron Centers Protein Ytfe and its Interaction with No
Chemistry, 22:9768-, 2016

PubMed Abstract: Molecular mechanisms underlying the repair of nitrosylated [Fe-S] clusters by the microbial protein YtfE remain poorly understood. The X-ray crystal structure of YtfE, in combination with EPR, magnetic circular dichroism (MCD), UV, and (17) O-labeling electron spin echo envelope modulation measurements, show that each iron of the oxo-bridged Fe(II) -Fe(III) diiron core is coordinatively unsaturated with each iron bound to two bridging carboxylates and two terminal histidines in addition to an oxo-bridge. Structural analysis reveals that there are two solvent-accessible tunnels, both of which converge to the diiron center and are critical for capturing substrates. The reactivity of the reduced-form Fe(II) -Fe(II) YtfE toward nitric oxide demonstrates that the prerequisite for N2 O production requires the two iron sites to be nitrosylated simultaneously. Specifically, the nitrosylation of the two iron sites prior to their reductive coupling to produce N2 O is cooperative. This result suggests that, in addition to any repair of iron centers (RIC) activity, YtfE acts as an NO-trapping scavenger to promote the NO to N2 O transformation under low NO flux, which precedes nitrosative stress.

PubMed: 27246459
DOI: 10.1002/CHEM.201600990

実験手法

X-RAY DIFFRACTION (2.09 Å)