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      Structural insights into the molecular mechanism of ABC transporters

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      https://www.riss.kr/link?id=A105366484

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      다국어 초록 (Multilingual Abstract)

      ABC (ATP-binding cassette) transporters mediate the translocation of a large variety of molecules across lipid bilayers andare directly driven by energy from ATP hydrolysis. Since the first crystal structure of an ABC transporter, the E. coli vitaminB...

      ABC (ATP-binding cassette) transporters mediate the translocation of a large variety of molecules across lipid bilayers andare directly driven by energy from ATP hydrolysis. Since the first crystal structure of an ABC transporter, the E. coli vitaminB12 transporter BtuCD, was reported in 2002, over thirty structures of ABC proteins in different functional states have beendetermined by X-ray crystallography or by single particle cryo-electron microscopy reconstruction. In this review, structuraldetails of ABC transporters, the maltose transporter of Escherichia coli and the P-glycoprotein of Caenorhabditis elegans,are discussed to understand the molecular mechanism of ABC importers and exporters, respectively.

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      참고문헌 (Reference)

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      9 Kim, J., "Subnanometre-resolution electron cryomicroscopy structure of a heterodimeric ABC exporter" 517 : 396-400, 2015

      10 Ward, A. B., "Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain" 110 : 13386-13391, 2013

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      2 Grote, M., "Transmembrane signaling in the maltose ABC transporter MalFGK2-E: periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer" 284 : 17521-17526, 2009

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      78 Higgins, C. F., "A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria" 323 : 448-450, 1986

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