Secondary structure nucleation in peptides. Transition metal ion stabilized .alpha.-helices

Ghadiri, Mojtaba; Choi, Chel‐Jong

doi:10.1021/ja00160a054

Cited by 291 publications

(204 citation statements)

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“…Stabilizing interactions involving side chains almost always occur between i,i+4 residues, as discussed in chapter 1.2 and evidenced by other results (Ghardiri & Choi, 1990). Based upon NMR spectroscopy (discussed below) the conformations at 0°C and 25°C are identical for the first 17 residues; therefore, the stabilizing interaction occurs beyond residue 17.…”

supporting

confidence: 57%

Structures and related properties of helical, disulfide-stabilized peptides

Pagel

1993

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supporting

confidence: 57%

Structures and related properties of helical, disulfide-stabilized peptides

Pagel

1993

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“…1A) (7,8). Such i, i þ 4 diHis motifs have been used for the assembly and stabilization of metalloproteins and peptides through coordination of divalent transition metal ions (9)(10)(11)(12). We have previously shown that MBPC-1 self-assembles into discrete oligomeric structures upon metal coordination by the diHis motifs.…”

Section: Resultsmentioning

confidence: 99%

Metal templated design of protein interfaces

Salgado

Ambroggio

Brodin

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

132

156

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Metal coordination is a key structural and functional component of a large fraction of proteins. Given this dual role we considered the possibility that metal coordination may have played a templating role in the early evolution of protein folds and complexes. We describe here a rational design approach, Metal Templated Interface Redesign (MeTIR), that mimics the time course of a hypothetical evolutionary pathway for the formation of stable protein assemblies through an initial metal coordination event. Using a folded monomeric protein, cytochrome cb 562 , as a building block we show that its non-self-associating surface can be made self-associating through a minimal number of mutations that enable Zn coordination. The protein interfaces in the resulting Zn-directed, D 2 -symmetrical tetramer are subsequently redesigned, yielding unique protein architectures that self-assemble in the presence or absence of metals. Aside from its evolutionary implications, MeTIR provides a route to engineer de novo protein interfaces and metal coordination environments that can be tuned through the extensive noncovalent bonding interactions in these interfaces.evolution | metal coordination | protein self-assembly | protein-protein interactions | templating

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“…On the basis of previous studies regarding natural or engineered metal-binding sites, we rationalized that mutations of solvent-exposed residue pairs i and i þ 4 of a helix [50][51][52][53] or i and i þ 3 of a helixloop 37 to a pair of either histidine or cysteine residues would induce homooligomeric assemblies upon incubation with metal. Specifically, we predicted the metal site within these assemblies to take on a tetrahedral or octahedral coordination, in which the mutated histidines or cysteines among the molecules participate in the metal coordination.…”

Section: Rationale and Design Of Mutationsmentioning

confidence: 99%

An approach to crystallizing proteins by metal‐mediated synthetic symmetrization

Laganowsky

Zhao²,

Soriaga

et al. 2011

Protein Science

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Combining the concepts of synthetic symmetrization with the approach of engineering metal-binding sites, we have developed a new crystallization methodology termed metal-mediated synthetic symmetrization. In this method, pairs of histidine or cysteine mutations are introduced on the surface of target proteins, generating crystal lattice contacts or oligomeric assemblies upon coordination with metal. Metal-mediated synthetic symmetrization greatly expands the packing and oligomeric assembly possibilities of target proteins, thereby increasing the chances of growing diffraction-quality crystals. To demonstrate this method, we designed various T4 lysozyme (T4L) and maltose-binding protein (MBP) mutants and cocrystallized them with one of three metal ions: copper (Cu 21 ), nickel (Ni 21 ), or zinc (Zn 21 ). The approach resulted in 16 new crystal structures-eight for T4L and eight for MBP-displaying a variety of oligomeric assemblies and packing modes, representing in total 13 new and distinct crystal forms for these proteins. We discuss the potential utility of the method for crystallizing target proteins of unknown structure by engineering in pairs of histidine or cysteine residues. As an alternate strategy, we propose that the varied crystallization-prone forms of T4L or MBP engineered in this work could be used as crystallization chaperones, by fusing them genetically to target proteins of interest.

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Secondary structure nucleation in peptides. Transition metal ion stabilized .alpha.-helices

Abstract: 1989, 17. (d) Felix, A. M.; Heimer, E. P.; Wang, C.-T.; Lambros, T.-J.; Fournier, A.; Mowles, T. F.; Maines, S.; Campbell, R. M.; Wegrzynshi, B. B.; Toome, V.; Fry, D.; Madison, V. Int.

Cited by 291 publications

References 1 publication

Structures and related properties of helical, disulfide-stabilized peptides

Structures and related properties of helical, disulfide-stabilized peptides

Metal templated design of protein interfaces

An approach to crystallizing proteins by metal‐mediated synthetic symmetrization

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