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3FTJ

Crystal structure of the periplasmic region of MacB from Actinobacillus actinomycetemcomitans

3FTJ の概要
エントリーDOI10.2210/pdb3ftj/pdb
分子名称Macrolide export ATP-binding/permease protein macB (2 entities in total)
機能のキーワードmacrolide-specific pump, abc-type transporter, heat stable exotoxin ii, membrane protein, periplasmic region, antibiotic resistance, atp-binding, cell inner membrane, cell membrane, hydrolase, membrane, nucleotide-binding, transmembrane, transport
由来する生物種Actinobacillus actinomycetemcomitans (Haemophilus actinomycetemcomitans)
細胞内の位置Cell inner membrane; Multi-pass membrane protein (Potential): Q2EHL8
タンパク質・核酸の鎖数1
化学式量合計24726.88
構造登録者
Xu, Y.,Ha, N.C. (登録日: 2009-01-13, 公開日: 2009-05-26, 最終更新日: 2024-03-20)
主引用文献Xu, Y.,Sim, S.-H.,Nam, K.H.,Jin, X.L.,Kim, H.-M.,Hwang, K.Y.,Lee, K.,Ha, N.-C.
Crystal structure of the periplasmic region of MacB, a noncanonic ABC transporter
Biochemistry, 48:5218-5225, 2009
Cited by
PubMed Abstract: MacB is a noncanonic ABC-type transporter within Gram-negative bacteria, which is responsible both for the efflux of macrolide antibiotics and for the secretion of heat-stable enterotoxin II. In Escherichia coli, MacB requires the membrane fusion protein MacA and the multifunctional outer membrane channel TolC to pump substrates to the external medium. Sequence analysis of MacB suggested that MacB has a relatively large periplasmic region. To gain insight into how MacB assembles with MacA and TolC, we determined the crystal structure of the periplasmic region of Actinobacillus actinomycetemcomitans MacB. Fold matching program reveals that parts of the MacB periplasmic region have structural motifs in common with the RND-type transporter AcrB. Since it behaved as a monomer in solution, our finding is consistent with the dimeric nature of full-length MacB, providing an insight into the assembly in the tripartite efflux pump.
PubMed: 19432486
DOI: 10.1021/bi900415t
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.999 Å)
構造検証レポート
Validation report summary of 3ftj
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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