BtuB
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <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 cobalamin (a vitamin B12 derivative), lipid, methanesulfonothioate derivative and Ca+2 ions (green) (PDB code [[3m8d]])'> |
== Function == | == Function == | ||
| Line 7: | Line 7: | ||
== Structural highlights == | == Structural highlights == | ||
| - | BtuB depends on the presence of Ca+2 ions for high affinity binding of | + | BtuB depends on the presence of Ca+2 ions for high affinity binding of cobalamin (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 11:55, 12 November 2015
| |||||||||||
