2019
DOI: 10.1016/j.jinorgbio.2019.03.002
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Oligomerization of cytochrome c, myoglobin, and related heme proteins by 3D domain swapping

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Cited by 33 publications
(16 citation statements)
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“…During purification the highly hydrophobic OmcS (Qian et al, 2011) and other proteins are separated from the lipid-rich environment of the outer-cell surface and suspended in high salt and high pH aqueous solutions. Changes in chemical conditions are known to induce c -type cytochrome monomers to polymerize into nanowires (Hirota et al, 2010; Haldar et al, 2015; Alvarez De Eulate et al, 2017; Hirota, 2019; Nucara et al, 2019). An important stabilizing element in the OmcS filament structure is the coordination of a histidine in one subunit with the iron in the heme of an adjacent subunit (Filman et al, 2019; Wang et al, 2019).…”
Section: Introductionmentioning
confidence: 99%
“…During purification the highly hydrophobic OmcS (Qian et al, 2011) and other proteins are separated from the lipid-rich environment of the outer-cell surface and suspended in high salt and high pH aqueous solutions. Changes in chemical conditions are known to induce c -type cytochrome monomers to polymerize into nanowires (Hirota et al, 2010; Haldar et al, 2015; Alvarez De Eulate et al, 2017; Hirota, 2019; Nucara et al, 2019). An important stabilizing element in the OmcS filament structure is the coordination of a histidine in one subunit with the iron in the heme of an adjacent subunit (Filman et al, 2019; Wang et al, 2019).…”
Section: Introductionmentioning
confidence: 99%
“…Many c-type cyts can form oligomers by 3D domain swapping (herein, domain swapping) [3][4][5][6][7][8][9][10][11]. In domain swapping, two or more identical protein monomers exchange the same domain or secondary structural elements and fold into dimers or higher oligomers whose units are structurally similar to the original monomer [12][13][14][15]. Positively charged horse cytochrome (cyt) c forms domain-swapped oligomers by treatment with ethanol, and dimeric and trimeric horse cyt c are formed by swapping the Cterminal α-helix ( Fig.…”
Section: Introductionmentioning
confidence: 99%
“…The first is contact dimerization, when the loop of one of the monomers forms stabilizing contacts with another molecule; the second is terminal domain exchange or domain swapping [ 51 ]. Domain exchange is typical of proteins such as cytochrome c [ 52 ] and, in particular, some amyloidogenic proteins, such as human prion protein, cystatin C, or β 2 -microglobulin [ 53 , 54 ].…”
Section: Secreted Ribonucleases Of Bacillimentioning
confidence: 99%