Structural Basis of the Allosteric Behaviour of Phosphofructokinase

Overview

Journal Nature

Specialty Science

Date 1990 Jan 11

PMID 2136935

Citations 64

Authors

T Schirmer

P R Evans

Affiliations

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Abstract

Comparison between the crystal structures of low- and high-affinity forms of phosphofructokinase shows a close coupling between the change of quaternary structure and local changes triggered by binding of the allosteric effectors. These concerted changes link all the substrate and effector sites in the tetramer, and explain the change of affinity for the cooperative substrate.

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Structural basis for allosteric regulation of human phosphofructokinase-1.

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