X-ray structures of Ferritins and related proteins.
(2010) Biochimica et Biophysica Acta : international journal of biochemistry and biophysics — Vol. 1800, n° 8, p. 706-718 (2010)
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- Ferritins are members of a much larger superfamily of proteins, which are characterised by a structural motif consisting of a bundle of four parallel and anti-parallel alpha-helices. The ferritin super-family itself is widely distributed across all three living kingdoms, in both aerobic and anaerobic organisms, and a considerable number of X-ray structures are available, some at extremely high resolution. We describe first of all the subunit structure of mammalian H- and L-chain ferritins, and then discuss inter-subunit interactions in the 24-subunit quaternary structure of these ferritins. Bacteria contain two types of ferritins, FTNs, which like mammalian ferritins do not contain haem, and the haem-containing BFRs. The characteristic carboxylate-bridged di-iron ferroxidase sites of H-chain ferritins, FTNs and BFRs are compared, as are the potential entry sites for iron and the 'nucleation' site of L-chain ferritins. Finally we discuss the 3-dimensional structures of the 12-subunit bacterial Dps (DNA-binding protein from starved cells) proteins as well as their intersubunit di-iron ferroxidase site.
Citations
Crichton, R., & Declercq, J.-P. (2010). X-ray structures of Ferritins and related proteins. Biochimica et Biophysica Acta : international journal of biochemistry and biophysics, 1800(8), 706-718. https://doi.org/10.1016/j.bbagen.2010.03.019 (Original work published 2010)