TY - JOUR
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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U2 - 10.1074/jbc.M113.524421
DO - 10.1074/jbc.M113.524421
M3 - Article
C2 - 24573673
AN - SCOPUS:84899005526
SN - 0021-9258
VL - 289
SP - 11042
EP - 11058
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 16
ER -