BtuB
From Proteopedia
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| - | <StructureSection load='3m8d' size='450' side='right' scene= caption='E. coli BtuB complex with | + | <StructureSection load='3m8d' size='450' side='right' scene= caption='E. coli BtuB complex with cobalamine (a vitamin B12 derivative), lipid, methanesulfonothioate derivative and Ca+2 ions (green) (PDB code [[3m8d]])'> |
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| + | == 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. 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''' 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. | ||
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| + | == Structural highlights == | ||
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| + | BtuB depends on the presence of Ca+2 ions for high affinity binding of cobalamine (a form of vitamin B12). The Ca+2 ions are coordinated to several Asp side chains. | ||
==3D structure of BtuB== | ==3D structure of BtuB== | ||
Revision as of 11:45, 12 November 2015
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