BtuB: Difference between revisions
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BtuB depends on the presence of Ca+2 ions for high affinity <scene name='43/439262/Cv/2'>binding of cobalamin (a form of vitamin B12)</scene>. The <scene name='43/439262/Cv/3'>Ca+2 ions are coordinated to several Asp side chains</scene>.<ref>PMID:20816073</ref> | BtuB depends on the presence of Ca+2 ions for high affinity <scene name='43/439262/Cv/2'>binding of cobalamin (a form of vitamin B12)</scene>. The <scene name='43/439262/Cv/3'>Ca+2 ions are coordinated to several Asp side chains</scene>.<ref>PMID:20816073</ref> | ||
</StructureSection> | |||
==3D structure of BtuB== | ==3D structure of BtuB== | ||
Revision as of 10:46, 30 November 2015
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3D structure of BtuB
Updated on 30-November-2015
Colicins, 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