The dpsa-homologue of the archaeon halobacterium salinarum is a ferritin

Sabine Reindel; Stefan Anemüller; Andrzej Sawaryn; Berthold F. Matzanke

doi:10.1016/S0167-4838(02)00361-8

The dpsa-homologue of the archaeon halobacterium salinarum is a ferritin

Sabine Reindel, Stefan Anemüller, Andrzej Sawaryn, Berthold F. Matzanke^*

^*Corresponding author for this work

27 Citations (Scopus)

Abstract

An iron-rich protein, DpsA_Hsal, was isolated from the archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC7942. It consists of 20-kDa subunits forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 100 Fe ions per mole of holoprotein. CD spectra and secondary structure calculations are consistent with an

Original language	English
Journal	Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume	1598
Issue number	1-2
Pages (from-to)	140-146
Number of pages	7
ISSN	0167-4838
DOIs	https://doi.org/10.1016/S0167-4838(02)00361-8
Publication status	Published - 29.07.2002

Funding

This work is supported by DFG grant Ma 916/14-1.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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10.1016/S0167-4838(02)00361-8

Cite this

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abstract = "An iron-rich protein, DpsAHsal, was isolated from the archaeon Halobacterium salinarum sharing a sequence identity of 35\% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC7942. It consists of 20-kDa subunits forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 100 Fe ions per mole of holoprotein. CD spectra and secondary structure calculations are consistent with an",

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AU - Reindel, Sabine

AU - Anemüller, Stefan

AU - Sawaryn, Andrzej

AU - Matzanke, Berthold F.

PY - 2002/7/29

Y1 - 2002/7/29

N2 - An iron-rich protein, DpsAHsal, was isolated from the archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC7942. It consists of 20-kDa subunits forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 100 Fe ions per mole of holoprotein. CD spectra and secondary structure calculations are consistent with an

AB - An iron-rich protein, DpsAHsal, was isolated from the archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC7942. It consists of 20-kDa subunits forming a dodecameric structure. The protein exhibits a ferric iron loading of up to 100 Fe ions per mole of holoprotein. CD spectra and secondary structure calculations are consistent with an

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JO - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

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IS - 1-2

ER -

The dpsa-homologue of the archaeon halobacterium salinarum is a ferritin

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