TY - JOUR
T1 - The dpsa-homologue of the archaeon halobacterium salinarum is a ferritin
AU - Reindel, Sabine
AU - Anemüller, Stefan
AU - Sawaryn, Andrzej
AU - Matzanke, Berthold F.
N1 - Funding Information:
This work is supported by DFG grant Ma 916/14-1.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
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
UR - http://www.scopus.com/inward/record.url?scp=0037194405&partnerID=8YFLogxK
U2 - 10.1016/S0167-4838(02)00361-8
DO - 10.1016/S0167-4838(02)00361-8
M3 - Journal articles
C2 - 12147354
AN - SCOPUS:0037194405
SN - 0167-4838
VL - 1598
SP - 140
EP - 146
JO - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
JF - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
IS - 1-2
ER -
