Structural differences in d and l -monellin in the crystals of racemic mixture 1 1Edited by D. C. Rees

Hung, Li‐Wei; Kohmura, Masanori; Ariyoshi, Yasuo; Kim, Sung‐Hou

doi:10.1006/jmbi.1998.2308

Cited by 48 publications

(38 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The available set of racemic and quasiracemic protein crystal structures allows 14 comparisons with chiral crystal counterparts (8, 29, 32, 33, 35-39, 42, 43), and all seem to suggest that native tertiary structure is maintained. Only three racemate structures include specific native-like quaternary contacts (8,32,41). In one of these systems (32), native-like quaternary contacts are maintained.…”

Section: Resultsmentioning

confidence: 99%

“…We wondered whether this tetrameric assembly would be maintained under the conditions of racemic crystallization, a technique first implemented by Zawadzke and Berg (29) that has become increasingly popular in recent years (29)(30)(31)(32)(33)(34)(35)(36)(37)(38)(39)(40)(41)(42)(43)(44). It has been proposed that racemates are more prone to crystallization than single enantiomers because racemates can access achiral and centrosymmetric packing arrangements in the solid state (45), arrangements that are not available to a chiral entity.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

High-resolution structures of a heterochiral coiled coil

Mortenson

Steinkruger

Kreitler

et al. 2015

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

View full text Add to dashboard Cite

Interactions between polypeptide chains containing amino acid residues with opposite absolute configurations have long been a source of interest and speculation, but there is very little structural information for such heterochiral associations. The need to address this lacuna has grown in recent years because of increasing interest in the use of peptides generated from D amino acids (D peptides) as specific ligands for natural proteins, e.g., to inhibit deleterious proteinprotein interactions. Coiled-coil interactions, between or among α-helices, represent the most common tertiary and quaternary packing motif in proteins. Heterochiral coiled-coil interactions were predicted over 50 years ago by Crick, and limited experimental data obtained in solution suggest that such interactions can indeed occur. To address the dearth of atomic-level structural characterization of heterochiral helix pairings, we report two independent crystal structures that elucidate coiled-coil packing between L-and D-peptide helices. Both structures resulted from racemic crystallization of a peptide corresponding to the transmembrane segment of the influenza M2 protein. Networks of canonical knobs-into-holes side-chain packing interactions are observed at each helical interface. However, the underlying patterns for these heterochiral coiled coils seem to deviate from the heptad sequence repeat that is characteristic of most homochiral analogs, with an apparent preference for a hendecad repeat pattern.D peptides | transmembrane peptides | racemic crystallization | racemic detergent | coiled coil P olypeptides comprising D-amino acid residues have been sources of growing interest for biological applications, often for functions that depend on recognition by specific natural proteins (1-3). D peptides offer identical versatility in terms of conformation and side-chain functionality relative to conventional peptides (composed of L-amino acid residues), but D peptides are impervious to the action of proteolytic enzymes, which should improve pharmacokinetic properties in vivo relative to those of conventional peptides. The engineering of D peptides to display defined protein-binding preferences is hindered, however, by the dearth of experimental information available for such complexes. Structural principles that are well-known to govern interactions between two L-polypeptide chains are not directly extensible to pairings between peptides of opposite chirality. Favorable heterochiral interactions (between L-and D peptides) that are analogous to homochiral associations between L peptides were postulated decades ago on the basis of geometrical considerations (4, 5). In a 1953 analysis of structural parameters governing coiled-coil formation between right-handed α-helices formed from L peptides, for example, Crick suggested that analogous assemblies should be accessible to pairs of right-and left-handed helices (4). In the same year, Pauling and Corey postulated that heterochiral peptide mixtures could form "rippled" β-sheet assemblies with backbo...

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

High-resolution structures of a heterochiral coiled coil

Mortenson

Steinkruger

Kreitler

et al. 2015

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

View full text Add to dashboard Cite

show abstract

“…Although high-throughput robotics now makes it possible to screen vast numbers of crystallization conditions, some proteins remain recalcitrant to crystallization. Many approaches have been developed to improve the success rate for crystallization, for example, systematically truncating the target protein, 1,2 methylating the lysine residues, 3,4 removing post-translational modifications, [5][6][7] screening homologues of the target protein for crystallization, 8,9 fusing the target protein to a carrier protein, [10][11][12][13] crystallizing racemic mixtures of the target protein, [14][15][16][17][18][19][20] and cocrystallizing the target protein with antibodies or other binding proteins. [21][22][23] A number of those methods have been reviewed.…”

Section: Introductionmentioning

confidence: 99%

An approach to crystallizing proteins by metal‐mediated synthetic symmetrization

Laganowsky

Zhao²,

Soriaga

et al. 2011

Protein Science

View full text Add to dashboard Cite

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.

show abstract

“…17 It was also predicted that for racemic protein crystals, the space group, P1, would be the one most frequently observed 17 ; crystallographic experiments by us and by others have so far confirmed this prediction. 2,4,8,[18][19][20] The present study adds another example of a racemic protein crystal that is not in P1 but in another space group, P2 1 /c. 3 The number of proteins that have been crystallized in racemic form is still small, so an accurate statistical analysis of space groups is not possible yet.…”

Section: Discussionmentioning

confidence: 96%

Determination of the X‐ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography

et al. 2010

View full text Add to dashboard Cite

The 50-residue snake venom protein L-omwaprin and its enantiomer D-omwaprin were prepared by total chemical synthesis. Radial diffusion assays were performed against Bacillus megaterium and Bacillus anthracis; both L-and D-omwaprin showed antibacterial activity against B. megaterium. The native protein enantiomer, made of L-amino acids, failed to crystallize readily. However, when a racemic mixture containing equal amounts of L-and D-omwaprin was used, diffraction quality crystals were obtained. The racemic protein sample crystallized in the centrosymmetric space group P2 1 /c and its structure was determined at atomic resolution (1.33 Å ) by a combination of Patterson and direct methods based on the strong scattering from the sulfur atoms in the eight cysteine residues per protein. Racemic crystallography once again proved to be a valuable method for obtaining crystals of recalcitrant proteins and for determining highresolution X-ray structures by direct methods.

show abstract

Structural differences in d and l -monellin in the crystals of racemic mixture 1 1Edited by D. C. Rees

Cited by 48 publications

References 27 publications

High-resolution structures of a heterochiral coiled coil

High-resolution structures of a heterochiral coiled coil

An approach to crystallizing proteins by metal‐mediated synthetic symmetrization

Determination of the X‐ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography

Contact Info

Product

Resources

About