3D9B

Symmetric structure of E. coli AcrB

3D9B の概要

• エントリーDOI: 10.2210/pdb3d9b/pdb
• 関連するPDBエントリー: 2I6W
• 分子名称: Acriflavine resistance protein B, NICKEL (II) ION (2 entities in total)
• 機能のキーワード: alpha-helices, transmembrane protein, inner membrane, transport, transport protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P31224
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 113723.87

構造登録者

Veesler, D.,Blangy, S.,Cambillau, C.,Sciara, G. (登録日: 2008-05-27, 公開日: 2008-07-01, 最終更新日: 2023-08-30)

主引用文献

Veesler, D.,Blangy, S.,Cambillau, C.,Sciara, G.
There is a baby in the bath water: AcrB contamination is a major problem in membrane-protein crystallization.
Acta Crystallogr.,Sect.F, 64:880-885, 2008

PubMed Abstract: In the course of a crystallographic study of the Methanosarcina mazei CorA transporter, the membrane protein was obtained with at least 95% purity and was submitted to crystallization trials. Small crystals (<100 microm) were grown that diffracted to 3.42 A resolution and belonged to space group R32, with unit-cell parameters a = b = 145.74, c = 514.0 A. After molecular-replacement attempts using available CorA structures as search models failed to yield a solution, it was discovered that the crystals consisted of an Escherichia coli contaminating protein, acriflavine resistance protein B (AcrB), that was present at less than 5% in the protein preparations. AcrB contamination is a major problem when expressing membrane proteins in E. coli since it binds naturally to immobilized metal-ion affinity chromatography (IMAC) resins. Here, the structure is compared with previously deposited AcrB structures and strategies are proposed to avoid this contamination.

PubMed: 18931428
DOI: 10.1107/S1744309108028248

実験手法

X-RAY DIFFRACTION (3.42 Å)