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Differences between CusA and AcrB Crystallisation Highlighted by Protein Flexibility
BACKGROUND: Until very recently, AcrB was the only Resistance Nodulation and cell Division transporter for which the structure has been elucidated. Towards a general understanding of this protein family, CusA and AcrB were compared. METHODOLOGY/PRINCIPAL FINDINGS: In dodecylmaltoside, AcrB crystalli...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2704858/ https://www.ncbi.nlm.nih.gov/pubmed/19593437 http://dx.doi.org/10.1371/journal.pone.0006214 |
Sumario: | BACKGROUND: Until very recently, AcrB was the only Resistance Nodulation and cell Division transporter for which the structure has been elucidated. Towards a general understanding of this protein family, CusA and AcrB were compared. METHODOLOGY/PRINCIPAL FINDINGS: In dodecylmaltoside, AcrB crystallised in many different conditions, while CusA does not. This could be due to the difference in dynamic between these proteins as judged from limited proteolysis assays. Addition of various compounds, in particular heavy metal cations, stabilises CusA. CONCLUSION/SIGNIFICANCE: This approach could constitute a first step towards CusA crystallisation. |
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