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Literature summary for 7.6.2.8 extracted from

  • Weng, J.; Fan, K.; Wang, W.
    The conformational transition pathways of ATP-binding cassette transporter BtuCD revealed by targeted molecular dynamics simulation (2012), PLoS ONE, 7, e305465.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular dynamics simulations to explore the atomic details of the conformational transitions of BtuCD importer. The outward-facing to inward-facing transition is initiated by the conformational movement of nucleotide-binding domains. The subsequent reorientation of the substrate translocation pathway at transmembrane domains begins with the closing of the periplasmic gate, followed by the opening of the cytoplasmic gate in the last stage of the conformational transition due to the extensive hydrophobic interactions at this region, consistent with the functional requirement of unidirectional transport of the substrates. The reverse inward-facing to outward-facing transition exhibits intrinsic diversity of the conformational transition pathways and significant structural asymmetry Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P06611 subunit BtuD
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Synonyms

Synonyms Comment Organism
BtuCD
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Escherichia coli