BtuB
From Proteopedia
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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> | ||
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==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
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
References
- ↑ Chimento DP, Kadner RJ, Wiener MC. The Escherichia coli outer membrane cobalamin transporter BtuB: structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation. J Mol Biol. 2003 Oct 3;332(5):999-1014. PMID:14499604 doi:http://dx.doi.org/10.1016/S0022283603009975
- ↑ Freed DM, Horanyi PS, Wiener MC, Cafiso DS. Conformational exchange in a membrane transport protein is altered in protein crystals. Biophys J. 2010 Sep 8;99(5):1604-10. PMID:20816073 doi:10.1016/j.bpj.2010.06.026
