BtuB
From Proteopedia
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== Function == | == Function == | ||
| - | '''BtuB''' is an outer membrane receptor found in a variety of bacteria, such as ''E. coli''. BtuB transports vitamin B12 across the membrane of gram-negative bacteria. The transport is achieved with high affinity by the collaboration of BtuB and the periplasmic protein TonB. <ref>PMID:14499604</ref> As an essential receptor for the cell that is constitutively expressed, it is an ideal target to be parasitized, a feature exploited by a variety of proteins such as [[Colicin]]s. | + | '''BtuB'''or '''vitamin B12 receptor''' or '''outer membrane cobalamin transporter''' is an outer membrane receptor found in a variety of bacteria, such as ''E. coli''. BtuB transports vitamin B12 across the membrane of gram-negative bacteria. The transport is achieved with high affinity by the collaboration of BtuB and the periplasmic protein TonB. <ref>PMID:14499604</ref> As an essential receptor for the cell that is constitutively expressed, it is an ideal target to be parasitized, a feature exploited by a variety of proteins such as [[Colicin]]s. |
== Structural highlights == | == Structural highlights == | ||
Revision as of 11:26, 6 November 2022
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References
- ↑ Chimento DP, Kadner RJ, Wiener MC. 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. 2003 Oct 3;332(5):999-1014. PMID:14499604 doi:http://dx.doi.org/10.1016/S0022283603009975
- ↑ Freed DM, Horanyi PS, Wiener MC, Cafiso DS. Conformational exchange in a membrane transport protein is altered in protein crystals. Biophys J. 2010 Sep 8;99(5):1604-10. PMID:20816073 doi:10.1016/j.bpj.2010.06.026
