Structure of the apo form of Bacillus stearothermophilus phosphofructokinase.
The crystal structure of the unliganded form of Bacillus stearothermophilus phosphofructokinase (BsPFK) was determined using molecular replacement to 2.8 Å resolution (Protein Data Bank entry  3U39 ). The apo BsPFK structure serves as the basis for the interpretation of any structural changes seen in the binary or ternary complexes. When the apo BsPFK structure is compared with the previously published liganded structures of BsPFK, the structural impact that the binding of the ligands produces is revealed. This comparison shows that the apo form of BsPFK resembles the substrate-bound form of BsPFK, a finding that differs from previous predictions.
Department of Biochemistry and Biophysics, Texas A&M University and Texas AgriLife Research, College Station, Texas 77843-2128, United States.
Rockann
R
Mosser
Manchi C M
MC
Reddy
John B
JB
Bruning
James C
JC
Sacchettini
Gregory D
GD
Reinhart
D000494:Allosteric Regulation / Q000235:genetics; D001051:Apoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018360:Crystallography, X-Ray; D005636:Fructosephosphates / Q000737:chemistry / Q000378:metabolism; D001411:Geobacillus stearothermophilus / Q000201:enzymology* / Q000235:genetics; D008024:Ligands; D025221:Phosphofructokinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding / Q000235:genetics; D013379:Substrate Specificity / Q000235:genetics
D001051:Apoenzymes; D001426:Bacterial Proteins; D005636:Fructosephosphates; D008024:Ligands; C027618:fructose-6-phosphate; D025221:Phosphofructokinases