Structure of the Apo Form of Bacillus Stearothermophilus Phosphofructokinase

Overview

Journal Biochemistry

Specialty Biochemistry

Date 2012 Jan 4

PMID 22212099

Citations 4

Authors

Rockann Mosser

Manchi C M Reddy

John B Bruning

James C Sacchettini

Gregory D Reinhart

Affiliations

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Abstract

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.

Citing Articles

The effect of introducing small cavities on the allosteric inhibition of phosphofructokinase from Bacillus stearothermophilus.

Whitaker A, Reinhart G Arch Biochem Biophys. 2016; 607:1-6.

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Enhancing allosteric inhibition in Thermus thermophilus Phosphofructokinase.

McGresham M, Reinhart G Biochemistry. 2014; 54(3):952-8.

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Allosteric regulation in phosphofructokinase from the extreme thermophile Thermus thermophilus.

McGresham M, Lovingshimer M, Reinhart G Biochemistry. 2013; 53(1):270-8.

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Redefining the role of the quaternary shift in Bacillus stearothermophilus phosphofructokinase.

Mosser R, Reddy M, Bruning J, Sacchettini J, Reinhart G Biochemistry. 2013; 52(32):5421-9.

PMID: 23859543 PMC: 3785328. DOI: 10.1021/bi4002503.

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