BtuB: Difference between revisions

New page: 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 ...
 
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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.
<StructureSection load='3m8d' size='450' side='right' scene='43/439262/Cv/1' caption='E. coli BtuB complex with cobalamin (a vitamin B12 derivative), lipid, methanesulfonothioate derivative and Ca+2 ions (green) (PDB code [[3m8d]])'>


{{STRUCTURE_2guf | PDB=2guf |  SCENE= }}
== Function ==
 
'''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 ==
 
BtuB depends on the presence of Ca+2 ions for high affinity <scene name='43/439262/Cv/6'>binding of cobalamin (a form of vitamin B12)</scene>. The <scene name='43/439262/Cv/7'>Ca+2 ions are coordinated to several Asp side chains</scene>.<ref>PMID:20816073</ref>
 
==3D structure of BtuB==
[[BtuB 3D structures]]
 
</StructureSection>
 
 
== References ==
<references/>
[[Category:Topic Page]]

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Gemma McGoldrick, Michal Harel, Alexander Berchansky