Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CusBopen access
- Authors
- Xu, Yongbin; Yun, Bo-Young; Sim, Se-Hoon; Lee, Kangseok; Ha, Nam-Chul
- Issue Date
- Jul-2009
- Publisher
- International Union of Crystallography
- Keywords
- Gram-negative bacteria; Membrane-fusion proteins; Metal-efflux pumps; RND-type transporters
- Citation
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v.65, no.7, pp 743 - 745
- Pages
- 3
- Journal Title
- Acta Crystallographica Section F: Structural Biology and Crystallization Communications
- Volume
- 65
- Number
- 7
- Start Page
- 743
- End Page
- 745
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/23131
- DOI
- 10.1107/S1744309109019873
- ISSN
- 1744-3091
2053-230X
- Abstract
- Periplasmic membrane-fusion proteins (MFPs) are an essential component of multidrug and metal-efflux pumps in Gram-negative bacteria. However, the functional structure of MFPs remains unclear. CusCFBA, the Cu-I and Ag-I efflux system in Escherichia coli, consists of the MFP CusB, the OMF CusC and the RND-type transporter CusA. The MFP CusB bridges the inner membrane RND-type efflux transporter CusA and the outer membrane factor CusC and exhibits substrate-linked conformational changes which distinguish it from other MFP-family members. CusB from E. coli was overexpressed and the recombinant protein was purified using Ni-NTA affinity, Q anion-exchange and gel-filtration chromatography. The purified CusB protein was crystallized using the vapour-diffusion method. A diffraction data set was collected to a resolution of 3.1 angstrom at 100 K. The crystal belonged to space group C222.
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