Structure of the apo form of Bacillus stearothermophilus phosphofructokinase. Academic Article

abstract

• The crystal structure of the unliganded form of Bacillus stearothermophilus phosphofructokinase (BsPFK) was determined using molecular replacement to 2.8 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.

authors

• Reinhart, Gregory
• Sacchettini, James

published proceedings

• Biochemistry

author list (cited authors)

• Mosser, R., Reddy, M., Bruning, J. B., Sacchettini, J. C., & Reinhart, G. D.

citation count

• 8

complete list of authors

• Mosser, Rockann||Reddy, Manchi CM||Bruning, John B||Sacchettini, James C||Reinhart, Gregory D

publication date

• January 2012

publisher

• American Chemical Society (ACS)  Publisher

published in

• Biochemistry  Journal

keywords

• Allosteric Regulation
• Apoenzymes
• Bacterial Proteins
• Crystallography, X-Ray
• Fructosephosphates
• Geobacillus Stearothermophilus
• Ligands
• Phosphofructokinases
• Protein Binding
• Substrate Specificity

PubMed Central ID

• 22212099

Digital Object Identifier (DOI)

• 10.1021/bi201548p

start page

• 769

end page

• 775

volume

• 51

issue

• 3

URL

• http://dx.doi.org/10.1021/bi201548p