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The First Three-Dimensional Structure of Phosphofructokinase from Saccharomyces cerevisiae Determined by Electron Microscopy of Single Particles

Phosphofructokinaseis a key regulatory enzyme of the glycolytic pathway. We have determined the structure of this enzyme from Saccharomyces cerevisiae to a resolution of 2.0 nm. This is the first structure available for this family of enzymes in eukaryotic organisms. Phosphofructokinase is an octame...

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Published in:Journal of structural biology 2001-12, Vol.136 (3), p.167-180
Main Authors: Ruiz, Teresa, Kopperschläger, Gerhard, Radermacher, Michael
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creator Ruiz, Teresa
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description Phosphofructokinaseis a key regulatory enzyme of the glycolytic pathway. We have determined the structure of this enzyme from Saccharomyces cerevisiae to a resolution of 2.0 nm. This is the first structure available for this family of enzymes in eukaryotic organisms. Phosphofructokinase is an octamer composed of 4α and 4β subunits arranged in a dihedral point group symmetry D2. The enzyme has a very open and elongated structure, with dimensions of 24 nm in length and 17 nm in width. The final structure, calculated from 0° tilt projections of the molecule at random orientations using as reference the volume obtained by the random conical reconstruction technique in ice, has allowed us to discern the shapes of the subunits and their mutual arrangement in the octamer.
doi_str_mv 10.1006/jsbi.2002.4440
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identifier ISSN: 1047-8477
ispartof Journal of structural biology, 2001-12, Vol.136 (3), p.167-180
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1095-8657
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subjects CTF correction
electron microscopy
glycolytic enzyme
Microscopy, Electron - methods
Models, Molecular
phosphofructokinase
Phosphofructokinase-1 - chemistry
Phosphofructokinase-1 - ultrastructure
Protein Conformation
Protein Subunits
radon transforms
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
simultaneous alignment
three-dimensional reconstruction
vitreous ice
title The First Three-Dimensional Structure of Phosphofructokinase from Saccharomyces cerevisiae Determined by Electron Microscopy of Single Particles
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