論文

査読有り
2010年3月

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

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
  • Kanako Terakado
  • ,
  • Atsushi Kodan
  • ,
  • Hiroaki Nakano
  • ,
  • Yasuhisa Kimura
  • ,
  • Kazumitsu Ueda
  • ,
  • Toru Nakatsu
  • ,
  • Hiroaki Kato

66
3
開始ページ
319
終了ページ
323
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1107/S0907444909055504
出版者・発行元
WILEY-BLACKWELL PUBLISHING, INC

An MsbA deletion mutant Delta C21 that lacks the two C-terminal alpha-helices was expressed in Escherichia coli strain C41 and purified by metal-affinity and gel-filtration chromatography. Purified Delta C21 retained 26% of the activity of the wild-type ATPase and had a similar binding affinity to fluorescent nucleotide derivatives. Although crystals of wild-type MsbA complexed with adenosine 5'-(beta,gamma-imido) triphosphate could not be obtained, crystals of Delta C21 that diffracted to 4.5 angstrom resolution were obtained. The preliminary Delta C21 structure had the outward-facing conformation, in contrast to the previously reported E. coli MsbA structure. This result suggests that deletion of the C-terminal alpha-helices may play a role in facilitating the outward-facing nucleotide-bound crystal structure of EcMsbA.

リンク情報
DOI
https://doi.org/10.1107/S0907444909055504
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/20179345
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000274536400013&DestApp=WOS_CPL
ID情報
  • DOI : 10.1107/S0907444909055504
  • ISSN : 0907-4449
  • PubMed ID : 20179345
  • Web of Science ID : WOS:000274536400013

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