Deleting two C-terminal α-helices is effective to crystallize the bacterial ABC transporter Escherichia coli MsbA complexed with AMP-PNP

An MsbA deletion mutant ΔC21 that lacks the two C‐terminal α‐helices was expressed in Escherichia coli strain C41 and purified by metal‐affinity and gel‐filtration chromatography. Purified ΔC21 retained 26% of the activity of the wild‐type ATPase and had a similar binding affinity to fluorescent nuc...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2010-03, Vol.66 (3), p.319-323
Hauptverfasser:	Terakado, Kanako, Kodan, Atsushi, Nakano, Hiroaki, Kimura, Yasuhisa, Ueda, Kazumitsu, Nakatsu, Toru, Kato, Hiroaki
Format:	Artikel
Sprache:	eng
Schlagworte:	ABC exporters Adenylyl Imidodiphosphate - chemistry Adenylyl Imidodiphosphate - metabolism Amino Acid Sequence ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - metabolism Bacterial Proteins - chemistry Bacterial Proteins - metabolism crystal-packing arrangement Crystallography, X-Ray Escherichia coli - chemistry Escherichia coli - metabolism membrane proteins Models, Molecular Molecular Sequence Data MsbA Protein Binding Protein Structure, Quaternary Protein Structure, Secondary Protein Structure, Tertiary Sequence Alignment
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