Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4XGA

Crystal structure of BamB and BamA P3-5 complex from E.coli

4XGA の概要
エントリーDOI10.2210/pdb4xga/pdb
分子名称Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamA, CALCIUM ION, ... (4 entities in total)
機能のキーワードouter member protein, protein binding-membrane protein complex, protein binding/membrane protein
由来する生物種Escherichia coli (strain K12)
詳細
細胞内の位置Cell outer membrane ; Lipid-anchor : P77774
Cell outer membrane : P0A940
タンパク質・核酸の鎖数2
化学式量合計68065.00
構造登録者
Chen, Z.,Zhan, L.H.,Dong, C.,Gao, Z.Q.,Dong, Y.H. (登録日: 2014-12-30, 公開日: 2016-01-20, 最終更新日: 2023-11-08)
主引用文献Chen, Z.,Zhan, L.H.,Hou, H.F.,Gao, Z.Q.,Xu, J.H.,Dong, C.,Dong, Y.H.
Structural basis for the interaction of BamB with the POTRA3-4 domains of BamA.
Acta Crystallogr D Struct Biol, 72:236-244, 2016
Cited by
PubMed Abstract: In Escherichia coli, the Omp85 protein BamA and four lipoproteins (BamBCDE) constitute the BAM complex, which is essential for the assembly and insertion of outer membrane proteins into the outer membrane. Here, the crystal structure of BamB in complex with the POTRA3-4 domains of BamA is reported at 2.1 Å resolution. Based on this structure, the POTRA3 domain is associated with BamB via hydrogen-bonding and hydrophobic interactions. Structural and biochemical analysis revealed that the conserved residues Arg77, Glu127, Glu150, Ser167, Leu192, Leu194 and Arg195 of BamB play an essential role in interaction with the POTRA3 domain.
PubMed: 26894671
DOI: 10.1107/S2059798315024729
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.15 Å)
構造検証レポート
Validation report summary of 4xga
検証レポート(詳細版)ダウンロードをダウンロード

252456

件を2026-04-22に公開中

PDB statisticsPDBj update infoContact PDBjnumon