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Literature summary for 7.6.2.8 extracted from

  • Pan, C.; Weng, J.; Wang, W.
    ATP hydrolysis induced conformational changes in the vitamin B12 transporter BtuCD revealed by MD simulations (2016), PLoS ONE, 11, e0166980 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.6.2.8

Localization

Localization Comment Organism GeneOntology No. Textmining
cell membrane transmembrane enzyme Escherichia coli
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inner membrane transmembrane enzyme Escherichia coli
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-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] Escherichia coli
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 ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P06609 AND P06611 AND P37028 genes btuC, btuD, and btuF encoding for vitamin B12 import system permease protein BtuC, vitamin B12 import ATP-binding protein BtuD, and vitamin B12-binding protein BtuF
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1]
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 Escherichia coli ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
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 ?

Subunits

Subunits Comment Organism
homodimer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
BtuCD
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 Escherichia coli
BtuCD-F complex
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 Escherichia coli
vitamin B12 transporter
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 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
additional information post-hydrolysis state of the vitamin B12 importer BtuCD by molecular dynamics (MD) simulations, overview. Predominantly asymmetric arrangement of the NBD dimer interface, with the ADP-bound site disrupted and the ATP-bound site preserved in most of the trajectories. TMDs response to ATP hydrolysis by separation of the L-loops and opening of the cytoplasmic gate II, indicating that hydrolysis of one ATP facilitates substrate translocation by opening the cytoplasmic end of translocation pathway. Motions of the L-loops and the cytoplasmic gate II are coupled with each other through a contiguous interaction network involving a conserved Asn83 on the extended stretch preceding transmembrane (TM)3 helix plus the cytoplasmic end of TM2/6/7 helix bundle. TMD-NBD communication mechanism for type II ABC importers. Besides the four basic domains of BtuCD, a cognate periplasmic binding protein, BtuF, is also required to maximize transport rate. Different conformational states of BtuCD, and mechanism of B12 transport cycle in BtuCD, overview. The occluded state of BtuCD, occ-BtuCD (PDB ID 4FI3), is regarded as a crucial step of the transport cycle, in which the transporter simultaneously loads the shipment B12 and the energy source ATPs. Transition from the occ-BtuCD state to the inward-facing state after ATP hydrolysis Escherichia coli
physiological function vitamin B12 importer BtuCD is a type II ATP binding cassette (ABC) importer mediating the uptake of vitamin B12 across the inner membrane. ABC transporters utilize the energy of ATP hydrolysis to unidirectionally transport substrates across cell membrane. ATP hydrolysis occurs at the nucleotide-binding domain (NBD) dimer interface of ABC transporters, whereas substrate translocation takes place at the translocation pathway between the transmembrane domains (TMDs), which is more than 30 A away from the NBD dimer interface Escherichia coli