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 journalArticle

12 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 languageEnglish (US)
Pages (from-to)11042-11058
Number of pages17
JournalJournal of Biological Chemistry
Volume289
Issue number16
DOIs
StatePublished - Apr 18 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Williams, S. M., Chandran, A. V., Vijayabaskar, M. S., Roy, S., Balaram, H., Vishveshwara, S., Vijayan, M., & Chatterji, D. (2014). A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis. Journal of Biological Chemistry, 289(16), 11042-11058. https://doi.org/10.1074/jbc.M113.524421