Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter

ATP binding cassette (ABC) transporters mediate vital transport processes in every living cell. ATP hydrolysis, which fuels transport, displays positive cooperativity in numerous ABC transporters. In particular, heterodimeric ABC exporters exhibit pronounced allosteric coupling between a catalytical...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2014-07, Vol.111 (30), p.11025-11030
Hauptverfasser:	Hohl, Michael, Hürlimann, Lea M., Böhm, Simon, Schöppe, Jendrik, Grütter, Markus G., Bordignon, Enrica, Seeger, Markus A.
Format:	Artikel
Sprache:	eng
Schlagworte:	ABC transporters adenosine Adenosine Monophosphate - analogs & derivatives Adenosine Monophosphate - chemistry Adenosine Monophosphate - genetics Adenosine Monophosphate - metabolism Adenosine triphosphatase Adenosine triphosphatases adenosine triphosphate Adenosine Triphosphate - chemistry Adenosine Triphosphate - genetics Adenosine Triphosphate - metabolism alanine Allosteric Regulation - physiology Allosteric Site aspartic acid ATP binding cassette transporters ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - genetics ATP-Binding Cassette Transporters - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding sites Biological Sciences Biological Transport, Active - physiology Cells crosslinking Crystal structure Crystals Dimers Exporters Hydrogen bonds Hydrolysis Lactococcus lactis - chemistry Lactococcus lactis - genetics Lactococcus lactis - metabolism Molecular structure Mutation Nucleotides Protein Structure, Secondary Protein Structure, Tertiary
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