The structure of cat muscle pyruvate kinase.

Muirhead, H.; Clayden, D. A.; Barford, David; Lorimer, C.G.; Fothergill‐Gilmore, Linda A.; Schiltz, Emile; Schmitt, Wilfried

doi:10.1002/j.1460-2075.1986.tb04236.x

Cited by 255 publications

(194 citation statements)

References 32 publications

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“…The X-ray diffraction studies on cat M1 PK [6] have revealed the complex molecular architecture of the enzyme, which is a tetramer of four identical subunits, each encompassing three domains (see Fig. 2A The reaction is catalysed by pyruvate kinase (PK), which requires for its activity both monovalent and divalent cations [1,2].…”

Section: Overall Architecturementioning

confidence: 99%

“…Glycolysis; Metabolism regulation; X-ray crystallography; Pyruvate kinase whereas the L PK is additionally controlled by phosphorylation on a N-terminal Ser residue which causes a decrease in the affinity for the PEP and FBP activators [3]. More unusual is the muscle M1 protein [6] which is the only known PK displaying hyperbolic kinetics and no allosteric control.While the structure of the cat M1 isoenzyme was determined by Muirhead and coworkers several years ago [6], little information was available about the allosteric transition in PK. Substantial progress in this respect has been observed over the last few years with further refinement of the M1 isoenzyme model [7], and with the X-ray structure determination of the FBP-dependent E. coli PK, in the inactive T-state [8].…”

mentioning

confidence: 99%

mentioning

confidence: 99%

“…More unusual is the muscle M1 protein [6] which is the only known PK displaying hyperbolic kinetics and no allosteric control.…”

mentioning

confidence: 99%

“…While the structure of the cat M1 isoenzyme was determined by Muirhead and coworkers several years ago [6], little information was available about the allosteric transition in PK. Substantial progress in this respect has been observed over the last few years with further refinement of the M1 isoenzyme model [7], and with the X-ray structure determination of the FBP-dependent E. coli PK, in the inactive T-state [8].…”

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confidence: 99%

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The allosteric regulation of pyruvate kinase

1996

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Crystallographic and mutagenesis studies have unravelled the general features of the allosteric transition mechanism in pyruvate kinase. The enzyme displays a dramatic conformational change in going from the T-to the R-state. All three domains forming each subunit of the tetrameric enzyme undergo simultaneous and concerted rotations, in such a way that all subunit and domain interfaces are modified. This mechanism is unprecedented since in all tetrameric allosteric enzymes, characterised at atomic resolution, at least one of the domain or subunit interfaces remains unchanged on the T-to R-state transition. The molecular mechanism of allosteric regulation here proposed provides a rationale for the effect of single site mutations observed in the human erythrocyte pyruvate kinase associated with a congenital anaemia.Key words." Glycolysis; Metabolism regulation; X-ray crystallography; Pyruvate kinase whereas the L PK is additionally controlled by phosphorylation on a N-terminal Ser residue which causes a decrease in the affinity for the PEP and FBP activators [3]. More unusual is the muscle M1 protein [6] which is the only known PK displaying hyperbolic kinetics and no allosteric control.While the structure of the cat M1 isoenzyme was determined by Muirhead and coworkers several years ago [6], little information was available about the allosteric transition in PK. Substantial progress in this respect has been observed over the last few years with further refinement of the M1 isoenzyme model [7], and with the X-ray structure determination of the FBP-dependent E. coli PK, in the inactive T-state [8]. Furthermore, insight into the enzyme regulatory properties has been provided by mutagenesis studies [9] and by the characterisation of several R PK variants from patients with congenital anaemia [10].

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Section: Overall Architecturementioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

“…More unusual is the muscle M1 protein [6] which is the only known PK displaying hyperbolic kinetics and no allosteric control.…”

mentioning

confidence: 99%

mentioning

confidence: 99%

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The allosteric regulation of pyruvate kinase

1996

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Structural trees for protein superfamilies

Ефимов

1997

Proteins

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Structural trees for large protein superfamilies, such as beta proteins with the aligned beta sheet packing, beta proteins with the orthogonal packing of alpha helices, two-layer and three-layer alpha/beta proteins, have been constructed. The structural motifs having unique overall folds and a unique handedness are taken as root structures of the trees. The larger protein structures of each superfamily are obtained by a stepwise addition of alpha helices and/or beta strands to the corresponding root motif, taking into account a restricted set of rules inferred from known principles of the protein structure. Among these rules, prohibition of crossing connections, attention to handedness and compactness, and a requirement for alpha helices to be packed in alpha-helical layers and beta strands in beta layers are the most important. Proteins and domains whose structures can be obtained by stepwise addition of alpha helices and/or beta strands to the same root motif can be grouped into one structural class or a superfamily. Proteins and domains found within branches of a structural tree can be grouped into subclasses or subfamilies. Levels of structural similarity between different proteins can easily be observed by visual inspection. Within one branch, protein structures having a higher position in the tree include the structures located lower. Proteins and domains of different branches have the structure located in the branching point as the common fold.

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