Protein Family Models

The Plug domain has been shown to be an independently folding subunit of the TonB-dependent receptors ([1]). It acts as the channel gate, blocking the pore until the channel is bound by ligand. At this point it under goes conformational changes opens the channel. [1]. 15111112. The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane beta-barrel. Oke M, Sarra R, Ghirlando R, Farnaud S, Gorringe AR, Evans RW, Buchanan SK;. FEBS Lett 2004;564:294-300. (from Pfam)

Date:

2024-10-16

This entry represents the beta-barrel domain of TonB-dependent receptors, such as BtuB, CirA, FatA, FcuT, FecA, FepA, among others [1]. [1]. 9886293. Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Buchanan SK, Smith BS, Venkatramani L, Xia D, Esser L, Palnitkar M, Chakraborty R, van der Helm D, Deisenhofer J;. Nat Struct Biol 1999;6:56-63. (from Pfam)

Date:

2024-10-16

TonB-dependent vitamin B12 receptor BtuB is involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space

Date:

2019-06-17

Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space

Gene:

btuB

Date:

2021-09-03

This model represents the TonB-dependent outer membrane receptor found in gamma proteobacteria responsible for translocating the cobalt-containing vitamin B12 (cobalamin) [1].

Gene:

btuB

Date:

2021-05-12