- EMDB-7286: Cryo-EM density map of Alternative Complex III from Flavobacteriu... -
+
データを開く
IDまたはキーワード:
読み込み中...
-
基本情報
登録情報
データベース: EMDB / ID: EMD-7286
タイトル
Cryo-EM density map of Alternative Complex III from Flavobacterium johnsoniae (Wild Type)
マップデータ
Structure of Alternative Complex III from Flavobacterium johnsoniae (Wild Type), primary map
試料
複合体: ACIII-cyt aa3 supercomplex
タンパク質・ペプチド: x 4種
タンパク質・ペプチド: x 2種
リガンド: x 5種
キーワード
Electron transport chain (電子伝達系) / triacylated cysteine / heme c domain / iron-sulfur cluster (鉄・硫黄クラスター) / MEMBRANE PROTEIN (膜タンパク質)
機能・相同性
機能・相同性情報
membrane => GO:0016020 / electron transfer activity / heme binding / metal ion binding / 細胞膜 類似検索 - 分子機能
Menaquinone reductase, multiheme cytochrome c subunit / NrfD family / Alternative complex III, ActD subunit / MoCo/4Fe-4S cofactor protein extended Tat translocation domain / Polysulphide reductase, NrfD / Alternative complex III, ActD subunit / : / Cytochrome c7-like / Cytochrome c7 and related cytochrome c / Multiheme cytochrome c family profile. ...Menaquinone reductase, multiheme cytochrome c subunit / NrfD family / Alternative complex III, ActD subunit / MoCo/4Fe-4S cofactor protein extended Tat translocation domain / Polysulphide reductase, NrfD / Alternative complex III, ActD subunit / : / Cytochrome c7-like / Cytochrome c7 and related cytochrome c / Multiheme cytochrome c family profile. / Cytochrome C oxidase, cbb3-type, subunit III / Multiheme cytochrome superfamily / シトクロムc / 4Fe-4S dicluster domain / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain 類似検索 - ドメイン・相同性
Uncharacterized protein / Cytochrome c, class I / 4Fe-4S ferredoxin, iron-sulfur binding domain protein / Polysulphide reductase, NrfD / Uncharacterized protein / Hypothetical lipoprotein 類似検索 - 構成要素
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)
R01-HL16101
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
P41-GM104601
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
U54-GM087519
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01-GM123455
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM103310
米国
National Institutes of Health/Office of the Director
OD019994
米国
Simons Foundation
349247
米国
Canadian Institutes of Health Research (CIHR)
MOP-81294
カナダ
引用
ジャーナル: Nature / 年: 2018 タイトル: Structure of the alternative complex III in a supercomplex with cytochrome oxidase. 著者: Chang Sun / Samir Benlekbir / Padmaja Venkatakrishnan / Yuhang Wang / Sangjin Hong / Jonathan Hosler / Emad Tajkhorshid / John L Rubinstein / Robert B Gennis / 要旨: Alternative complex III (ACIII) is a key component of the respiratory and/or photosynthetic electron transport chains of many bacteria. Like complex III (also known as the bc complex), ACIII ...Alternative complex III (ACIII) is a key component of the respiratory and/or photosynthetic electron transport chains of many bacteria. Like complex III (also known as the bc complex), ACIII catalyses the oxidation of membrane-bound quinol and the reduction of cytochrome c or an equivalent electron carrier. However, the two complexes have no structural similarity. Although ACIII has eluded structural characterization, several of its subunits are known to be homologous to members of the complex iron-sulfur molybdoenzyme (CISM) superfamily , including the proton pump polysulfide reductase. We isolated the ACIII from Flavobacterium johnsoniae with native lipids using styrene maleic acid copolymer, both as an independent enzyme and as a functional 1:1 supercomplex with an aa-type cytochrome c oxidase (cyt aa). We determined the structure of ACIII to 3.4 Å resolution by cryo-electron microscopy and constructed an atomic model for its six subunits. The structure, which contains a [3Fe-4S] cluster, a [4Fe-4S] cluster and six haem c units, shows that ACIII uses known elements from other electron transport complexes arranged in a previously unknown manner. Modelling of the cyt aa component of the supercomplex revealed that it is structurally modified to facilitate association with ACIII, illustrating the importance of the supercomplex in this electron transport chain. The structure also resolves two of the subunits of ACIII that are anchored to the lipid bilayer with N-terminal triacylated cysteine residues, an important post-translational modification found in numerous prokaryotic membrane proteins that has not previously been observed structurally in a lipid bilayer.