A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis

Sunanda Margrett Williams; Anu V. Chandran; Mahalingam S. Vijayabaskar; Sourav Roy; Hemalatha Balaram; Saraswathi Vishveshwara; Mamannamana Vijayan; Dipankar Chatterji

doi:10.1074/jbc.M113.524421

A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis

Sunanda Margrett Williams
, Anu V. Chandran
, Mahalingam S. Vijayabaskar
, Sourav Roy
, Hemalatha Balaram
, Saraswathi Vishveshwara
, Mamannamana Vijayan
, Dipankar Chatterji

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

Background: DNA-binding protein from starved cells (Dps) are nano-compartments that can oxidize and store iron rendering protection from free radicals. Results: A histidine-aspartate ionic cluster in mycobaterial Dps2 modulates the rate of iron entry and exit in these proteins. Conclusion: Substitutions that disrupt the cluster interface alter the iron uptake/release properties with localized structural changes. Significance: Identifying important gating residues can help in designing nano-delivery vehicles.

Original language	English (US)
Pages (from-to)	11042-11058
Number of pages	17
Journal	Journal of Biological Chemistry
Volume	289
Issue number	16
DOIs	https://doi.org/10.1074/jbc.M113.524421
State	Published - Apr 18 2014
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M113.524421

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title = "A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis",

abstract = "Background: DNA-binding protein from starved cells (Dps) are nano-compartments that can oxidize and store iron rendering protection from free radicals. Results: A histidine-aspartate ionic cluster in mycobaterial Dps2 modulates the rate of iron entry and exit in these proteins. Conclusion: Substitutions that disrupt the cluster interface alter the iron uptake/release properties with localized structural changes. Significance: Identifying important gating residues can help in designing nano-delivery vehicles.",

author = "Williams, \{Sunanda Margrett\} and Chandran, \{Anu V.\} and Vijayabaskar, \{Mahalingam S.\} and Sourav Roy and Hemalatha Balaram and Saraswathi Vishveshwara and Mamannamana Vijayan and Dipankar Chatterji",

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doi = "10.1074/jbc.M113.524421",

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T1 - A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis

AU - Williams, Sunanda Margrett

AU - Chandran, Anu V.

AU - Vijayabaskar, Mahalingam S.

AU - Roy, Sourav

AU - Balaram, Hemalatha

AU - Vishveshwara, Saraswathi

AU - Vijayan, Mamannamana

AU - Chatterji, Dipankar

PY - 2014/4/18

Y1 - 2014/4/18

N2 - Background: DNA-binding protein from starved cells (Dps) are nano-compartments that can oxidize and store iron rendering protection from free radicals. Results: A histidine-aspartate ionic cluster in mycobaterial Dps2 modulates the rate of iron entry and exit in these proteins. Conclusion: Substitutions that disrupt the cluster interface alter the iron uptake/release properties with localized structural changes. Significance: Identifying important gating residues can help in designing nano-delivery vehicles.

AB - Background: DNA-binding protein from starved cells (Dps) are nano-compartments that can oxidize and store iron rendering protection from free radicals. Results: A histidine-aspartate ionic cluster in mycobaterial Dps2 modulates the rate of iron entry and exit in these proteins. Conclusion: Substitutions that disrupt the cluster interface alter the iron uptake/release properties with localized structural changes. Significance: Identifying important gating residues can help in designing nano-delivery vehicles.

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UR - https://www.scopus.com/pages/publications/84899005526#tab=citedBy

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DO - 10.1074/jbc.M113.524421

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AN - SCOPUS:84899005526

SN - 0021-9258

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SP - 11042

EP - 11058

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 16

ER -

A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis

Abstract

ASJC Scopus subject areas

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