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BtuB

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{{STRUCTURE_2guf| PDB=2guf | SIZE=400| SCENE= |right|CAPTION=Structure of BtuB complex with monooleoyl-rac-glycerol and formate, [[2guf]] }}
{{STRUCTURE_2guf| PDB=2guf | SIZE=400| SCENE= |right|CAPTION=Structure of BtuB complex with monooleoyl-rac-glycerol and formate, [[2guf]] }}
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'''BtuB''' is an outer membrane receptor found in a variety of bacteria, such as ''E. coli''. 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.
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'''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. 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.

Revision as of 11:15, 12 November 2015

Template:STRUCTURE 2guf

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. 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 Colicins.



3D structure of BtuB

Updated on 12-November-2015

2guf, 1nqe, 1nqf – EcBtuB – Escherichia coli
3m8b, 3rgm, 3rgn – EcBtuB (mutant)
3m8d - EcBtuB (mutant) + cyanocobalamin
1nqh - EcBtuB + cyanocobalamin + Ca
2ysu - EcBtuB + Colicin E2 receptor binding domain
1ujw - EcBtuB + Colicin E3 receptor binding domain
2gsk - EcBtuB + TonB C-terminal
1nqg - EcBtuB + Ca
2bto – PdBtuBA + thioredoxin – Prosthecobacter dejongeii
2btq – PdBtuBA + PdBtuBB

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Michal Harel, Alexander Berchansky, Gemma McGoldrick

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