Interfacial metal coordination in engineered protein and peptide assemblies

Sontz, Pamela A.; Song, Woon Ju; Tezcan, F.A.

doi:10.1016/j.cbpa.2013.12.013

Cited by 81 publications

(74 citation statements)

References 65 publications

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“…Moreover, these assemblies can be highly sensitive to sequence and mutation. These difficulties have motivated the experimental use of interactions that are more easily programmed at protein interfaces, such as metal coordination ( 32 ), to drive intermolecular assembly.…”

Section: Introductionmentioning

confidence: 99%

Computationally designed peptides for self-assembly of nanostructured lattices

et al. 2016

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Section: Introductionmentioning

confidence: 99%

Computationally designed peptides for self-assembly of nanostructured lattices

et al. 2016

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“…[1][2][3][4][5][6][7][8][9][10][11][12] Remarkably, heme proteins use the same heme group to confer such diverse functions. myoglobin, Mb and hemoglobin, Hb), electron transfer (e.g.…”

Section: Introductionmentioning

confidence: 99%

“…[1][2][3][4][5][6][7][8][9][10][11][12] Recently, inspired by the novel His-heme cross-link in the truncated Hb family, cyanobacteria Synechocystis sp. [1][2][3][4][5][6][7][8][9][10][11][12] Recently, inspired by the novel His-heme cross-link in the truncated Hb family, cyanobacteria Synechocystis sp.…”

Section: Introductionmentioning

confidence: 99%

How a novel tyrosine–heme cross-link fine-tunes the structure and functions of heme proteins: a direct comparitive study of L29H/F43Y myoglobin

Yan

Yuan

et al. 2015

Dalton Trans.

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A heme-protein cross-link is a key post-translational modification (PTM) of heme proteins. Meanwhile, the structural and functional consequences of heme-protein cross-links are not fully understood, due to limited studies on a direct comparison of the same protein with and without the cross-link. A Tyr-heme cross-link with a C-O bond is a newly discovered PTM of heme proteins, and is spontaneously formed in F43Y myoglobin (Mb) between the Tyr hydroxyl group and the heme 4-vinyl group in vivo. In this study, we found that with an additional distal His29 introduced in the heme pocket, the double mutant L29H/F43Y Mb can form two distinct forms under different protein purification conditions, with and without a novel Tyr-heme cross-link. By solving the X-ray structures of both forms of L29H/F43Y Mb and performing spectroscopic studies, we made a direct structural and functional comparison in the same protein scaffold. It revealed that the Tyr-heme cross-link regulates the heme distal hydrogen-bonding network, and fine-tunes not only the spectroscopic and ligand binding properties, but also the protein reactivity. Moreover, the formation of the Tyr-heme cross-link in the double mutant L29H/F43Y Mb was investigated in vitro. This study addressed the key issue of how Tyr-heme cross-link fine-tunes the structure and functions of the heme protein, and provided a plausible mechanism for the formation of the newly discovered Tyr-heme cross-link.

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“…[1][2][3] Assemblies,s uch as cages,t ubes,a nd frameworks show great potential for use as molecular scaffolds and for development of catalysts,o ptical materials,a nd magnetic materials when metal complexes or metal ions are accumulated in the unique environments by metal coordination and chemical modification of amino acids. [4][5][6][7] These composites,w hich have large numbers of metal compounds appropriately aligned on or within the scaffolds,s how ah igh reactivity when externally stimulated, for example,b yl ight irradiation.…”

mentioning

confidence: 99%

A Photoactive Carbon‐Monoxide‐Releasing Protein Cage for Dose‐Regulated Delivery in Living Cells

et al. 2015

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Protein cages can serve as bioinorganic molecular templates for functionalizing metal compounds to regulate cellular signaling. We succeeded in developing a photoactive CO-releasing system by constructing a composite of ferritin (Fr) containing manganese-carbonyl complexes. When Arg52 adjacent to Cys48 of Fr is replaced with Cys, the Fr mutant stabilizes the retention of 48 Mn-carbonyl moieties, which can release the CO ligands under light irradiation, although wild-type Fr retains very few Mn moieties. The amount of released CO is regulated by the extent of irradiation. This could reveal an optimized dose for cooperatively activating the nuclear factor κB (NF-κB) in mammalian cells and the tumor necrosis factor α (TNF-α). These results suggest that construction of a CO-releasing protein cage will advance of research in CO biology.

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Interfacial metal coordination in engineered protein and peptide assemblies

Cited by 81 publications

References 65 publications

Computationally designed peptides for self-assembly of nanostructured lattices

Computationally designed peptides for self-assembly of nanostructured lattices

How a novel tyrosine–heme cross-link fine-tunes the structure and functions of heme proteins: a direct comparitive study of L29H/F43Y myoglobin

A Photoactive Carbon‐Monoxide‐Releasing Protein Cage for Dose‐Regulated Delivery in Living Cells

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