Structure of bovine liver rhodanese

Ploegman, Jan H.; Drent, Gé; Kalk, Kor H.; Hól, Wim G. J.

doi:10.1016/0022-2836(78)90207-3

Cited by 172 publications

(63 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…1d), corresponding to a distance of 4.7 nm, in good agreement with the distance of 4.5 nm in the crystal structure. [9] In the unfolded state at 5 M guanidinium chloride (GdmCl), 〈E〉 scales with the sequence separation of the labeling sites (Fig. 1e,f), as expected.…”

Section: Molecular Chaperones Are An Essential Part Of the Cellular Msupporting

confidence: 70%

Probing Protein–Chaperone Interactions with Single‐Molecule Fluorescence Spectroscopy

et al. 2008

View full text Add to dashboard Cite

Molecular chaperones aid protein folding in the cell, but their effects on the conformation of the substrate protein have largely eluded experimental investigation. Single‐molecule fluorescence spectroscopy was used to extract structural and dynamic information from a protein–chaperone complex (see figure; yellow: rhodanase, blue: GroEL). This approach will aid in a more physical understanding of the role of cellular factors in protein folding.

show abstract

Section: Molecular Chaperones Are An Essential Part Of the Cellular Msupporting

confidence: 70%

Probing Protein–Chaperone Interactions with Single‐Molecule Fluorescence Spectroscopy

et al. 2008

View full text Add to dashboard Cite

show abstract

“…The data were evaluated on-line using threedimensional ellipsoid masking. The refined cell parameters were a = 15.6 nm, b = 4.9 nm, c = 4.23 nm, with p = 98.6", which is in good agreement with those of the native crystals [15]. Because of geometrical constraints of the detector, only 174.5" of the usual range of 180" for spacegroup C2 were measured by rotating around the a axis.…”

Section: Data Collectionsupporting

confidence: 64%

“…Using the procedure of Hamilton et al [33], these sets, together with the existing CAD4 native diffractometer data set [15], were scaled upon each other by the program SCALEKB of the BIOMOL protein structure determination package. A scale factor and an isotropic temperature factor were used for each set.…”

Section: Data Processing and Internal Scalingmentioning

confidence: 99%

See 1 more Smart Citation

Soaking in Cs₂SO₄ reveals a caesium‐aromatic interaction in bovine‐liver rhodanese

Kooystra

Kalk

Hól

1988

European Journal of Biochemistry

View full text Add to dashboard Cite

Soaking crystals of rhodanese (thiosulphate : cyanide sulphurtransferase) in 2 M caesium sulphate reveals three caesium binding sites of this enzyme. One of these had been described before as a binding site for sodium ions and is located in a cleft close to the active site. In this site the monovalent cation is coordinated by five oxygen atoms. The first additional binding site seems to be quite special. The caesium ion is bound to the phenyl ring of a tryptophan residue. It is further liganded by two oxygen atoms. The third binding site is a result of crystal packing effects: caesium is liganded by four oxygen atoms, provided by two rhodanese molecules and one sulphate ion.It is likely that the binding of caesium affects the fluorescence of the tryptophan residue with which it interacts. Such possible effects should also be kept in mind when caesium ions are used as a quencher in fluorescence studies of proteins in general.

show abstract

“…(B) In the mDHFR-rhodanese chimera, the C terminus of mDHFR (cyan) is joined to the N terminus of rhodanese (red) via a linker peptide (white) of 15 residues that contains His 6-tag. Rhodanese (29), EGFP (19), and mDHFR (30) are represented by ribbon diagrams of their crystal structures (Protein Data Bank codes 1RHD, 1EMA, and 1U70, respectively). In the case of mDHFR, the only available crystal structure corresponds to a mutant ternary complex.…”

Section: Resultsmentioning

confidence: 99%

Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner

Kipnis¹,

Papo²,

Haran

et al. 2007

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

View full text Add to dashboard Cite

The double-ring chaperonin GroEL mediates protein folding, in conjunction with its helper protein GroES, by undergoing ATPinduced conformational changes that are concerted within each heptameric ring. Here we have examined whether the concerted nature of these transitions is responsible for protein substrate release in an all-or-none manner. Two chimeric substrates were designed, each with two different reporter activities that were recovered after denaturation in GroES-dependent and independent fashions, respectively. The refolding of the chimeras was monitored in the presence of GroEL variants that undergo ATPinduced intraring conformational changes that are either sequential (F44W/D155A) or concerted (F44W). Our results show that release of a protein substrate from GroEL in a domain-by-domain fashion is favored when the intraring allosteric transitions of GroEL are sequential and not concerted.allostery ͉ chaperonins ͉ cooperativity ͉ protein folding T he Escherichia coli chaperonin GroEL is a molecular machine that assists protein folding by undergoing allosteric transitions between protein substrate binding and release states (for reviews, see refs. 1-3). It is made up of two homoheptameric rings, stacked back-to-back, with a cavity at each end (4) in which protein folding can take place in a confining and protective environment. GroEL functions in conjunction with a heptameric ring-shaped cochaperonin, GroES (5), that caps the cavity of the so-called cis ring (6), thereby triggering dissociation of bound protein substrates into the cavity. The allosteric transitions of GroEL are induced by ATP binding that occurs with positive cooperativity within rings and negative cooperativity between rings (7, 8). Experimental data (refs. 9 and 10 and G. Curien, J. Grason, and G. Lorimer, personal communication) and simulations (11) have shown that the intraring allosteric transitions of GroEL are concerted, in accordance with the Monod-WymanChangeux model of cooperativity (12), as proposed in the nested model (7). In contrast, the intraring allosteric transitions of the eukaryotic heterooligomeric chaperonin CCT were recently shown to occur in a sequential fashion (13) in accordance with the Koshland-Némethy-Filmer model of cooperativity (14). The implications of these different allosteric mechanisms for the folding function of chaperonins have not yet been explored.The work described here was undertaken to establish whether the concerted intraring ATP-induced allosteric transitions of GroEL facilitate simultaneous release of different parts of a bound protein substrate, as previously speculated (13). By contrast, it was suggested (13) that ATP-induced sequential conformational changes in CCT may facilitate sequential release and, as a result, domain-by-domain substrate folding. A powerful tool available for investigating this question is a wild-type variant of GroEL that contains a fluorescence reporter introduced by the F44W mutation and has the D155A substitution that converts its ATP-induced intraring allosteric t...

show abstract

Structure of bovine liver rhodanese

Cited by 172 publications

References 43 publications

Probing Protein–Chaperone Interactions with Single‐Molecule Fluorescence Spectroscopy

Probing Protein–Chaperone Interactions with Single‐Molecule Fluorescence Spectroscopy

Soaking in Cs₂SO₄ reveals a caesium‐aromatic interaction in bovine‐liver rhodanese

Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner

Contact Info

Product

Resources

About

Structure of bovine liver rhodanese

Cited by 172 publications

References 43 publications

Probing Protein–Chaperone Interactions with Single‐Molecule Fluorescence Spectroscopy

Probing Protein–Chaperone Interactions with Single‐Molecule Fluorescence Spectroscopy

Soaking in Cs2SO4 reveals a caesium‐aromatic interaction in bovine‐liver rhodanese

Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner

Contact Info

Product

Resources

About

Soaking in Cs₂SO₄ reveals a caesium‐aromatic interaction in bovine‐liver rhodanese