Quaternary structure of pig liver phosphofructokinase.

Foe, Lawrence G.; Trujillo, John L.

doi:10.1016/s0021-9258(19)70497-9

Cited by 17 publications

(10 citation statements)

References 31 publications

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“…2A) showed a homogeneous spread of individual particles that were interpreted to be PFK tetramers composed of pairs of dimer units separated by a narrow space. Higher polymers than tetramers were not observed in these images, which were similar to previously published EM patterns of rabbit muscle (1,28,44,45), chicken and pig liver (27,46), and human erythrocytes and muscle (1,47) PFKs. Reference free alignment, classification, and averaging of individual particles of human PFK-M showed an elongated molecule with apparent dimensions of 14.5 nm for the long axis and 9 nm for the short axis.…”

Section: Em Analysis Of Human Muscle and D Discodeum Pfksupporting

confidence: 90%

“…This intriguing feature was also detected in some of the former electron microscopic views of the enzyme from rabbit muscle by Hesterberg et al (28) and was interpreted to reflect a change in the orientation of the subdomains. Thus, the particle was concluded to possess D 2 symmetry, as proposed before for the PFK tetramer from pig liver (27). Surprisingly, our 3-D reconstruction of PFK-M (Fig.…”

Section: Discussionsupporting

confidence: 74%

“…The octameric structures of PFK from Saccharomyces cerevisiae determined by electron microscopy (EM) and cryo-EM (24 -26) showed the shape of the molecule in the presence of substrates and its organization into two tetramers, each of them composed of symmetrical dimers. Early micrographs of the mammalian tetramer suggested the presence of a D 2 symmetry along the long axis of the enzyme (27,28). In this study we have determined the EM structure of human PFK-M in the presence of Fru-6-P. Reconstruction of the 3-D structure of the enzyme and fitting the bacterial tetramer atomic X-ray structures into the EM volume described the architecture of the molecule and led us to elucidate the spatial location of key binding sites and the arrangement of the dimeric components within the tetrameric enzyme.…”

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confidence: 99%

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Electron microscopy analysis of mammalian phosphofructokinase reveals an unusual 3‐dimensional structure with significant implications for enzyme function

et al. 2010

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Phosphofructokinase is a sophisticated allosteric enzyme that is fundamental for the control of glycolysis. The structure of the bacterial enzyme is well characterized. However, little is known about the structural organization of the more complex enzyme from mammals. We have obtained the structure of human muscle phosphofructokinase in the presence of fructose 6‐phosphate at a resolution of 1.8 nm by electron microscopy (EM). Particles of the tetrameric enzyme corresponded to an elongated molecule (14.5 ×9nm) arranged into 2 dimeric subdomains. Image analysis and 3‐dimensional reconstruction showed the presence of a prominent channel in one of the dimers but not in the opposite one, revealing that they are in greatly different conformations. Fitting of bacterial structures into the EM model suggested disruption of the fructose 6‐phosphate catalytic and the fructose 2,6‐bisphophate allosteric sites in the cavity‐containing dimer. Therefore, the reported structure might have major implications for the function of mammalian phosphofructoki‐nase.—Arechaga, I., Martínez‐Costa, O. H., Ferreras, C., Carrascosa, J. L., Aragon, J. J. Electron microscopy analysis of mammalian phosphofructokinase reveals an unusual 3‐dimensional structure with significant implications for enzyme function. FASEB J. 24, 4960–4968 (2010). http://www.fasebj.org

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Section: Em Analysis Of Human Muscle and D Discodeum Pfksupporting

confidence: 90%

Section: Discussionsupporting

confidence: 74%

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confidence: 99%

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Electron microscopy analysis of mammalian phosphofructokinase reveals an unusual 3‐dimensional structure with significant implications for enzyme function

et al. 2010

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“…These findings reveal a new behavior of a key glycolytic enzyme with insights on spatial organization and isoform-specific glucose metabolism in cells. and Trujillo, 1980), and this study did not address three important unknowns: whether filament assembly is regulated, the alignment of PFKL tetramers within the filaments, and whether filament formation occurs in cells. We now resolve these unknowns by showing the regulated assembly of PFKL filaments, their higher-order quaternary structure determined from negative-stain electron micrographs, and the dynamic behavior of punctate PFKL-EGFP particles in cells quantified from time-lapse imaging.…”

Section: Introductionmentioning

confidence: 96%

The glycolytic enzyme phosphofructokinase-1 assembles into filaments

Webb

Dosey

Wittmann

et al. 2017

Journal of Cell Biology

112

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“…Follow-up studies using sedimentation, analytical ultracentrifugation, and fluorescence anisotropy also showed PFKL self-assemblies [5][6] . Finally, negative stain EM performed in 1980 showed these to be composed of filaments 77 , which was further investigated recently (Fig. 2b) 76 .…”

Section: Phosphofructokinase (Pfk)mentioning

confidence: 56%

Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation

2019

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Filament formation by non-cytoskeletal enzymes has been known for decades, yet only relatively recently has its wide-spread role in enzyme regulation and biology come to be appreciated. This comprehensive review summarizes what is known for each enzyme confirmed to form filamentous structures in vitro, and for the many that are known only to form large self-assemblies within cells. For some enzymes, studies describing both the in vitro filamentous structures and cellular self-assembly formation are also known and described. Special attention is paid to the detailed structures of each type of enzyme filament, as well as the roles the structures play in enzyme regulation and in biology. Where it is known or hypothesized, the advantages conferred by enzyme filamentation are reviewed. Finally, the similarities, differences, and comparison to the SgrAI system are also highlighted.3 Contents INTRODUCTION…………………………………………………………..4 STRUCTURALLY CHARACTERIZED ENZYME FILAMENTS…….5

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Quaternary structure of pig liver phosphofructokinase.

Cited by 17 publications

References 31 publications

Electron microscopy analysis of mammalian phosphofructokinase reveals an unusual 3‐dimensional structure with significant implications for enzyme function

Electron microscopy analysis of mammalian phosphofructokinase reveals an unusual 3‐dimensional structure with significant implications for enzyme function

The glycolytic enzyme phosphofructokinase-1 assembles into filaments

Structures, functions, and mechanisms of filament forming enzymes: a renaissance of enzyme filamentation

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