Flexible aspartates propel iron to the ferroxidation sites along pathways stabilized by a conserved arginine in Dps proteins from Mycobacterium smegmatis.

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Flexible aspartates propel iron to the ferroxidation sites along pathways stabilized by a conserved arginine in Dps proteins from Mycobacterium smegmatis.

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2017 nî lūn-bûn

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Flexible aspartates propel iro ...... from Mycobacterium smegmatis.

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Flexible aspartates propel iro ...... from Mycobacterium smegmatis.

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Flexible aspartates propel iro ...... from Mycobacterium smegmatis.

@en

Flexible aspartates propel iro ...... from Mycobacterium smegmatis.

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Flexible aspartates propel iro ...... from Mycobacterium smegmatis.

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Flexible aspartates propel iro ...... from Mycobacterium smegmatis.

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P1476

Flexible aspartates propel iro ...... from Mycobacterium smegmatis.

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P2093

Dipankar Chatterji

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Sunanda Margrett Williams

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P2860

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The multi-layered structure of Dps with a novel di-nuclear ferroxidase center

Crystal Structure of Plant Ferritin Reveals a Novel Metal Binding Site That Functions as a Transit Site for Metal Transfer in Ferritin

Structural studies on the second Mycobacterium smegmatis Dps: invariant and variable features of structure, assembly and function

The crystal structure of ferritin from Helicobacter pylori reveals unusual conformational changes for iron uptake

Structural characterization and biological implications of di-zinc binding in the ferroxidase center of Streptococcus pyogenes Dpr

Structural and thermodynamic characterization of metal ion binding in Streptococcus suis Dpr

Structure and Mechanism of Iron Translocation by a Dps Protein from Microbacterium arborescens

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685-698

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scholarly article

P356

10.1039/C7MT00008A

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P433

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P478

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2017-04-18T00:00:00Z

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28418062

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