Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase.

Pickover, Clifford A.; McKay, David; Engelman, Donald M.; Steitz, Thomas A.

doi:10.1016/s0021-9258(19)86488-8

Cited by 176 publications

(43 citation statements)

References 23 publications

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“…For q < 0.25A-1, these two spectra are very different and prove that the unfolded protein is much more extended than the native one. Using the Guinier approximation, the gyration radius, Rg, of the native protein is found to be (23.~0.5)A, in agreement with the value (23.15fl.16)A inferred from X-ray small-angle scattering [9]. For unfolded PGK the corresponding value is about 78A.…”

Section: Resultssupporting

confidence: 80%

Structure of proteins unfolded by guanidinium chloride

et al. 1993

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Section: Resultssupporting

confidence: 80%

Structure of proteins unfolded by guanidinium chloride

et al. 1993

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“…It was found that a rotation of 20-25° about the helix normal reduced the distance between the substrates from 12 A to about 5 A, a suitable distance for a dissociative mechanism (Mildvan 1979), at the same time introducing unsatisfactorily close interactions between only six amino acid residues, all associated with a single segment of polypeptide chain. The change in the radius of gyration calculated from this model was consistent with the change observed in the low-angle X-ray studies by Pickover al. (1979)* Stereo drawings of the PGK molecule before and after this conformational change are shown in figure 8.…”

Section: Echanism Of Actionsupporting

confidence: 89%

“…This logical imperative of the single crystal X-ray studies has received strong independent support from solution X-ray studies of PGK. Pickover et al (1979) have observed that the radius of gyration of the PGK molecule decreases by 1.09 A on the formation of the ternary substrate complex. This change is consistent with, and has been interpreted as, a substrate-induced conformational change that brings the two domains together in precisely the way demanded by the single-crystal X-ray studies.…”

Section: Echanism Of Actionmentioning

confidence: 99%

Phosphoglycerate kinase

김영진¹,

백상기²,

이주원³

et al. 1981

Phil. Trans. R. Soc. Lond. B

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Phosphoglycerate kinase catalyses the high-energy phosphoryl transfer of the acyl phosphate of 1,3-bisphosphoglycerate to ADP to produce ATP, a reaction requiring magnesium ions. The enzyme is widely distributed and apparently highly conserved as a monomer of molecular mass 45 000. X-ray studies of the enzymes from horse muscle and yeast, carried out in Oxford and Bristol respectively, have shown that the molecular structures of the two enzymes are almost identical. The most striking aspect of the structure is that the single polypeptide chain is organized into two separated domains composed of the N-terminal and C-terminal halves of the chain. Substrate binding studies and the determination of the complete amino acid sequence of the horse enzyme suggest that the nucleotide substrates and the phosphoglycerate substrates are bound to the C-domain and N-domain, respectively, in sites that are separated by about 12 A. In order to bring the two substrates together for catalysis, a hinge-bending conformational change involving helix rotation has been proposed, for which there is independent evidence from solution studies. Crystals of the ternary complex of the horse enzyme have been prepared that may contain the folded form of the enzyme.

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“…The catalytic site lies between the two domains of the subunit, with the substrates ATP and F6P bound to different domains, so the lack of change of kcat between the two conformational states of the enzyme (Blangy 1968) suggests that no substantial change of structure occurs in this region. This rules out the large relative movement of domains seen in hexokinase and phosphoglycerate kinase (Bennett & Steitz 1980;McDonald et al 1978;Banks et al 1979;Pickover al. 1979).…”

Section: Discussionmentioning

confidence: 99%

Phosphofructokinase: structure and control

Evans

Farrants

Hudson

1981

Phil. Trans. R. Soc. Lond. B

166

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Phosphofructokinase from Bacillus stearothermophilus shows cooperative kinetics with respect to the substrate fructose-6-phosphate (F6P), allosteric activation by ADP, and inhibition by phosphoenolpyruvate. The crystal structure of the active conformation of the enzyme has been solved to 2.4 A resolution, and three ligand-binding sites have been located. Two of these form the active site and bind the substrates F6P and ATP. The third site binds both allosteric activator and inhibitor. The complex of the enzyme with F6P and ADP has been partly refined at 2.4 A resolution, and a model of ATP has been built into the active site by using the refined model of ADP and a 6 A resolution map of bound 5'-adenylylimidodiphosphate (AMPPNP). The gamma-phosphate of ATP is close to the 1-hydroxyl of F6P, in a suitable position for in-line phosphoryl transfer. The binding of the phosphate of F6P involves two arginines from a neighbouring subunit in the tetramer, which suggests that a rearrangement of the subunits could explain the cooperativity of substrate binding. The activatory ADP is also bound by residues from two subunits.

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Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase.

Cited by 176 publications

References 23 publications

Structure of proteins unfolded by guanidinium chloride

Structure of proteins unfolded by guanidinium chloride

Phosphoglycerate kinase

Phosphofructokinase: structure and control

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