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4ISM

Crystal structure of ferritin from Pseudo-nitzschia multiseries soaked with zinc

Summary for 4ISM
Entry DOI10.2210/pdb4ism/pdb
Related4ISP 4ITT 4ITW 4IWJ 4IWK 4IXK
DescriptorFerritin, ZINC ION (3 entities in total)
Functional Keywordsferritin, transport protein
Biological sourcePseudo-nitzschia multiseries
Total number of polymer chains8
Total formula weight153028.93
Authors
Pfaffen, S.,Murphy, M.E.P. (deposition date: 2013-01-16, release date: 2013-03-20, Last modification date: 2017-11-15)
Primary citationPfaffen, S.,Abdulqadir, R.,Le Brun, N.E.,Murphy, M.E.
Mechanism of ferrous iron binding and oxidation by ferritin from a pennate diatom.
J.Biol.Chem., 288:14917-14925, 2013
Cited by
PubMed Abstract: A novel ferritin was recently found in Pseudo-nitzschia multiseries (PmFTN), a marine pennate diatom that plays a major role in global primary production and carbon sequestration into the deep ocean. Crystals of recombinant PmFTN were soaked in iron and zinc solutions, and the structures were solved to 1.65-2.2-Å resolution. Three distinct iron binding sites were identified as determined from anomalous dispersion data from aerobically grown ferrous soaked crystals. Sites A and B comprise the conserved ferroxidase active site, and site C forms a pathway leading toward the central cavity where iron storage occurs. In contrast, crystal structures derived from anaerobically grown and ferrous soaked crystals revealed only one ferrous iron in the active site occupying site A. In the presence of dioxygen, zinc is observed bound to all three sites. Iron oxidation experiments using stopped-flow absorbance spectroscopy revealed an extremely rapid phase corresponding to Fe(II) oxidation at the ferroxidase site, which is saturated after adding 48 ferrous iron to apo-PmFTN (two ferrous iron per subunit), and a much slower phase due to iron core formation. These results suggest an ordered stepwise binding of ferrous iron and dioxygen to the ferroxidase site in preparation for catalysis and a partial mobilization of iron from the site following oxidation.
PubMed: 23548912
DOI: 10.1074/jbc.M113.454496
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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건을2025-02-05부터공개중

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