- EMDB-39773: Cryo-EM structure of E.coli SPFH-NfeD family protein complex QmcA-YbbJ -
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基本情報
登録情報
データベース: EMDB / ID: EMD-39773
タイトル
Cryo-EM structure of E.coli SPFH-NfeD family protein complex QmcA-YbbJ
マップデータ
試料
複合体: QmcA-YbbJ complex
タンパク質・ペプチド: Protein QmcA
タンパク質・ペプチド: Inner membrane protein YbbJ
キーワード
complex / MEMBRANE PROTEIN
機能・相同性
機能・相同性情報
identical protein binding / plasma membrane 類似検索 - 分子機能
: / Band 7/stomatin-like, conserved site / Band 7 protein family signature. / NfeD-like, C-terminal domain / : / NfeD-like C-terminal, partner-binding domain / Stomatin/HflK/HflC family / Band 7 domain / SPFH domain / Band 7 family / prohibitin homologues ...: / Band 7/stomatin-like, conserved site / Band 7 protein family signature. / NfeD-like, C-terminal domain / : / NfeD-like C-terminal, partner-binding domain / Stomatin/HflK/HflC family / Band 7 domain / SPFH domain / Band 7 family / prohibitin homologues / Band 7/SPFH domain superfamily / Nucleic acid-binding, OB-fold 類似検索 - ドメイン・相同性
Protein QmcA / Inner membrane protein YbbJ 類似検索 - 構成要素
ジャーナル: Structure / 年: 2024 タイトル: Cryo-EM structure of the SPFH-NfeD family protein complex QmcA-YbbJ. 著者: Kwan Ann Tan / Zhu Qiao / Zachary Ze En Lim / Joshua Yi Yeo / Yonlada Yong / Phong Hoa Do / Rya Ero / Yong-Gui Gao / 要旨: The SPFH (stomatin, prohibitin, flotillin, and HflK/C) protein family is universally present and encompasses the evolutionarily conserved SPFH domain. These proteins are predominantly localized in ...The SPFH (stomatin, prohibitin, flotillin, and HflK/C) protein family is universally present and encompasses the evolutionarily conserved SPFH domain. These proteins are predominantly localized in lipid raft and implicated in various biological processes. The NfeD (nodulation formation efficiency D) protein family is often encoded in tandem with SPFH proteins, suggesting a close functional relationship. Here, we elucidate the cryoelectron microscopy (cryo-EM) structure of the Escherichia coli QmcA-YbbJ complex belonging to the SPFH and NfeD families, respectively. Our findings reveal that the QmcA-YbbJ complex forms an intricate cage-like structure composed of 26 copies of QmcA-YbbJ heterodimers. The transmembrane helices of YbbJ act as adhesive elements bridging adjacent QmcA molecules, while the oligosaccharide-binding domain of YbbJ encapsulates the SPFH domain of QmcA. Our structural study significantly contributes to understanding the functional role of the NfeD protein family and sheds light on the interplay between SPFH and NfeD family proteins.