Antiparallel Four-Stranded Coiled Coil Specified by a 3-3-1 Hydrophobic Heptad Repeat

Deng, Yiqun; Liu, Jie; Zheng, Qi; Eliezer, David; Kallenbach, Neville R.; Lu, Min

doi:10.1016/j.str.2005.10.010

Cited by 57 publications

(79 citation statements)

References 62 publications

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“…S1b), consistent with a well-folded complex having an extensive hydrophobic core. The melting temperature (apparent Tm = 40.6, 40.8 °C (n = 2)) was lower than those of other naturally occurring coiled-coil proteins (Tm > 60 °C) [26][27][28][29] , and unfolding of the mHv1/VSOP-cc coiled-coil was irreversible (Fig. 3d).…”

Section: Coiled-coil Assembly Domain Of Mhv1/vsop and Its Structurementioning

confidence: 85%

The cytoplasmic coiled-coil mediates cooperative gating temperature sensitivity in the voltage-gated H+ channel Hv1

et al. 2012

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Hv1/VsoP is a dimeric voltage-gated H + channel in which the gating of one subunit is reportedly coupled to that of the other subunit within the dimer. The molecular basis for dimer formation and intersubunit coupling, however, remains unknown. Here we show that the carboxy terminus ends downstream of the s4 voltage-sensor helix twist in a dimer coiled-coil architecture, which mediates cooperative gating. We also show that the temperature-dependent activation of H + current through Hv1/VsoP is regulated by thermostability of the coiled-coil domain, and that this regulation is altered by mutation of the linker between s4 and the coiled-coil. Cooperative gating within the dimer is also dependent on the linker structure, which circular dichroism spectrum analysis suggests is α-helical. our results indicate that the cytoplasmic coiled-coil strands form continuous α-helices with s4 and mediate cooperative gating to adjust the range of temperatures over which Hv1/VsoP operates.

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Section: Coiled-coil Assembly Domain Of Mhv1/vsop and Its Structurementioning

confidence: 85%

The cytoplasmic coiled-coil mediates cooperative gating temperature sensitivity in the voltage-gated H+ channel Hv1

et al. 2012

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“…a') in this figure and throughout the main text is used to indicate a residue on the opposite chain. B An antiparallel tetramer with a 3-3-1 repeat, as in Figure 2B and reference [14]. C A parallel seven-helix coiled coil with a 3-1-2-1 hydrophobic pattern, as in Figure 2D and reference [19].…”

Section: Discussionmentioning

confidence: 99%

“…A When all e positions are mutated to Val, departing from the canonical 3-4 repeat and creating a 3-3-1 hydrophobic repeat, the resulting sequence gives a parallel tetramer [15]. B When all g positions are substituted with either Val or Ala, also producing a 3-3-1 repeat, the result is an anti-parallel tetramer [14]. C A right-handed parallel coiled-coil tetramer [18].…”

Section: Discussionmentioning

confidence: 99%

“…For example, the Lu group has reported variants of the yeast GCN4 transcription factor coiled coil with hydrophobic substitutions at the e or g positions, generating 3-3-1 hydrophobic repeats. Four peptides with this pattern form homotetramers, although the structures show orientations and axial alignments that differ according to the substitutions made (Figure 2A-B) [14][15][16]. The GCN4 variants all contain an asparagine residue at one of the hydrophobic positions, and the hydrogen-bonding potential of this group is accommodated in a variety of ways.…”

Section: Novel Structures Switches and Functionsmentioning

confidence: 99%

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Structural specificity in coiled-coil interactions

Grigoryan

Keating

2008

Current Opinion in Structural Biology

260

283

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Coiled coils have a rich history in the field of protein design and engineering. Novel structures, such as the first 7-helix coiled coil, continue to provide surprises and insights. Large-scale data sets quantifying the influence of systematic mutations on coiled-coil stability are a valuable new asset to the area. Scoring methods based on sequence and/or structure can predict interaction preferences in coiled-coil-mediated bZIP transcription factor dimerization. Experimental and computational methods for dealing with the near-degeneracy of many coiled-coil structures appear promising for future design applications.

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“…The interdigitated helical backbones are offset by ϳ0.25 of a heptad repead, which, along with the short ϳ8 Å distance between the helical axes, is a characteristic of a ferritin-type Alacoil (11). Alacoils have been previously observed in designed protein sequences (12)(13)(14)(15). There are no interchain salt bridges between any of the peptides in the octamers (Fig.…”

Section: Resultsmentioning

confidence: 88%

Crystal structure of a self-assembling lipopeptide detergent at 1.20 Å

Pomroy²,

Cuesta-Seijo³

et al. 2008

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

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Lipopeptide detergents (LPDs) are a new class of amphiphile designed specifically for the structural study of integral membrane proteins. The LPD monomer consists of a 25-residue peptide with fatty acyl chains linked to side chains located at positions 2 and 24 of the peptide. LPDs are designed to form ␣-helices that selfassemble into cylindrical micelles, providing a more natural interior acyl chain packing environment relative to traditional detergents. We have determined the crystal structure of LPD-12, an LPD coupled to two dodecanoic acids, to a resolution of 1.20 Å. The LPD-12 monomers adopt the target conformation and associate into cylindrical octamers as expected. Pairs of helices are strongly associated as Alacoil-type antiparallel dimers, and four of these dimers interact through much looser contacts into assemblies with approximate D 2 symmetry. The aligned helices form a cylindrical shell with a hydrophilic exterior that protects an interior hydrophobic cavity containing the 16 LPD acyl chains. Over 90% of the methylene/methyl groups from the acylated side chains are visible in the micelle interiors, and Ϸ90% of these adopt trans dihedral angle conformations. Dodecylmaltoside (DDM) was required for the crystallization of LPD-12, and we find 10 -24 ordered DDM molecules associated with each LPD assembly, resulting in an overall micelle molecular weight of Ϸ30 kDa. The structures confirm the major design objectives of the LPD framework, and reveal unexpected features that will be helpful in the engineering additional versions of lipopeptide amphiphiles.de novo protein design ͉ detergent design ͉ membrane proteins ͉ self-assembling amphiphiles ͉ x-ray crystallography D etergents that are able to stabilize native structures of membrane proteins in the absence of lipid bilayers are essential tools for the structural study of membrane proteins (1, 2). Despite the large number of detergents that are available, no single detergent is optimal for all purposes, and choice of the solubilizing agent is highly dependent on both the target protein and on the application. In particular, the structural study of membrane proteins by NMR or x-ray crystallography depends critically on the choice of detergent (3, 4), and many proteins cannot be studied because of problems with protein stability and aggregation in the commonly used detergents (5). Because of these issues, there is a need to expand the range of amphiphiles available for membrane proteins research.Nondenaturing detergents act as membrane mimetics, and an ideal detergent would generate a local environment at the protein surface that is indistinguishable from that of the native lipid bilayer. A central shortcoming of many of the commonly used detergents is that the micelle interior is less ordered and less well-packed relative to the interiors of lipid bilayers (2, 6). This is a direct result of the shape of the amphiphile monomer, which has a high degree of positive intrinsic curvature, resulting in self-assembly into spherical or ellipsoidal micelles with...

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Antiparallel Four-Stranded Coiled Coil Specified by a 3-3-1 Hydrophobic Heptad Repeat

Cited by 57 publications

References 62 publications

The cytoplasmic coiled-coil mediates cooperative gating temperature sensitivity in the voltage-gated H+ channel Hv1

The cytoplasmic coiled-coil mediates cooperative gating temperature sensitivity in the voltage-gated H+ channel Hv1

Structural specificity in coiled-coil interactions

Crystal structure of a self-assembling lipopeptide detergent at 1.20 Å

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