6pfk
PHOSPHOFRUCTOKINASE, INHIBITED T-STATE
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OverviewOverview
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.
About this StructureAbout this Structure
6PFK is a Single protein structure of sequence from Geobacillus stearothermophilus with as ligand. This structure supersedes the now removed PDB entry 5PFK. The following page contains interesting information on the relation of 6PFK with [The Glycolytic Enzymes]. Active as 6-phosphofructokinase, with EC number 2.7.1.11 Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of the allosteric behaviour of phosphofructokinase., Schirmer T, Evans PR, Nature. 1990 Jan 11;343(6254):140-5. PMID:2136935
Page seeded by OCA on Thu Feb 21 19:16:40 2008