Outer membrane receptor

Last updated
TonB dependent receptor
1qfg opm.png
Structure of ferric hydroxamate uptake receptor. [1]
Identifiers
SymbolTonB_dep_Rec
Pfam PF00593
Pfam clan CL0193
InterPro IPR000531
PROSITE PDOC00354
SCOP2 2fcp / SCOPe / SUPFAM
TCDB 1.B.14
OPM superfamily 33
OPM protein 1qfg
CDD cd01347
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Outer membrane receptors, also known as TonB-dependent receptors, are a family of beta barrel proteins named for their localization in the outer membrane of gram-negative bacteria. TonB complexes sense signals from the outside of bacterial cells and transmit them into the cytoplasm, leading to transcriptional activation of target genes. TonB-dependent receptors in gram-negative bacteria are associated with the uptake and transport of large substrates such as iron siderophore complexes and vitamin B12. [2]

Contents

TonB interactions with other proteins

In Escherichia coli , the TonB protein interacts with outer membrane receptor proteins that carry out high-affinity binding and energy-dependent uptake of specific substrates into the periplasmic space. [3] These substrates are either poorly transported through non-specific porin channels or are encountered at very low concentrations. In the absence of TonB, these receptors bind their substrates but do not carry out active transport. TonB-dependent regulatory systems consist of six protein protein components. [4]

The proteins that are currently known or presumed to interact with TonB include BtuB, [5] CirA, FatA, FcuT, FecA, [6] FhuA, [7] FhuE, FepA, [8] FptA, HemR, IrgA, IutA, PfeA, PupA, LbpA and TbpA. The TonB protein also interacts with some colicins. Most of these proteins contain a short conserved region at their N-terminus. [9]

TonB-dependent receptor plug domain

TonB-dependent Receptor Plug Domain
Identifiers
SymbolPlug
Pfam PF07715
InterPro IPR012910
SCOP2 1fi1 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

TonB-dependent receptors include a plug domain, an independently folding subunit that acts as the channel gate, blocking the pore until the channel is bound by ligand. At this point it undergoes conformational changes, opening the channel. [10]

TonB as phage receptor

TonB also acts as a receptor for Salmonella bacteriophage H8. In fact, H8 infection is TonB dependent. [11]

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References

  1. ↑ Ferguson AD, Welte W, Hofmann E, et al. (June 2000). "A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins". Structure. 8 (6): 585–92. doi: 10.1016/S0969-2126(00)00143-X . PMID   10873859.
  2. ↑ Koebnik, Ralf (2000). "Structures and function of bacterial outer membrane proteins: barrels in a nutshell". MicroReview. 37 (2): 239–253.
  3. ↑ Kadner RJ, Chimento DP, Wiener MC (2003). "The Escherichia coli outer membrane cobalamin transporter BtuB: structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation". J. Mol. Biol. 332 (5): 999–1014. doi:10.1016/j.jmb.2003.07.005. PMID   14499604.
  4. ↑ Koebnik R (2005). "TonB-dependent trans-envelope signalling: the exception or the rule?". Trends Microbiol. 13 (8): 343–7. doi:10.1016/j.tim.2005.06.005. PMID   15993072.
  5. ↑ Kadner RJ, Chimento DP, Wiener MC, Mohanty AK (2003). "Substrate-induced transmembrane signaling in the cobalamin transporter BtuB". Nat. Struct. Biol. 10 (5): 394–401. doi:10.1038/nsb914. PMID   12652322. S2CID   24883519.
  6. ↑ Deisenhofer J, Smith BS, Esser L, Chakraborty R, van der Helm D, Ferguson AD (2002). "Structural basis of gating by the outer membrane transporter FecA". Science. 295 (5560): 1715–1719. Bibcode:2002Sci...295.1715F. doi:10.1126/science.1067313. PMID   11872840. S2CID   86844549.
  7. ↑ Moras D, Rosenbusch JP, Mitschler A, Rees B, Locher KP, Koebnik R, Moulinier L (1998). "Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes". Cell. 95 (6): 771–778. doi: 10.1016/S0092-8674(00)81700-6 . PMID   9865695. S2CID   16899072.
  8. ↑ Deisenhofer J, Xia D, Buchanan SK, Smith BS, Venkatramani L, Esser L, Palnitkar M, Chakraborty R, van der Helm D (1999). "Crystal structure of the outer membrane active transporter FepA from Escherichia coli". Nat. Struct. Biol. 6 (1): 56–63. doi:10.1038/4931. PMID   9886293. S2CID   20231287.
  9. ↑ Klebba PE (2003). "Three paradoxes of ferric enterobactin uptake". Front. Biosci. 8 (6): s1422–s1436. doi:10.2741/1233. PMID   12957833.
  10. ↑ Buchanan SK, Evans RW, Ghirlando R, Oke M, Sarra R, Farnaud S, Gorringe AR (2004). "The plug domain of a neisserial TonB-dependent transporter retains structural integ rity in the absence of its transmembrane beta-barrel". FEBS Lett. 564 (3): 294–300. doi: 10.1016/S0014-5793(04)00196-6 . PMID   15111112. S2CID   20056753.
  11. ↑ Rabsch, W.; Ma, L.; Wiley, G.; Najar, F. Z.; Kaserer, W.; Schuerch, D. W.; Klebba, J. E.; Roe, B. A.; Laverde Gomez, J. A. L.; Schallmey, M.; Newton, S. M. C.; Klebba, P. E. (2007). "FepA- and TonB-Dependent Bacteriophage H8: Receptor Binding and Genomic Sequence". Journal of Bacteriology. 189 (15): 5658–5674. doi:10.1128/JB.00437-07. PMC   1951831 . PMID   17526714.


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