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Structure of the apo form of Bacillus stearothermophilus phosphofructokinase.

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.

SUBMITTER: Mosser R

PROVIDER: S-EPMC3285294 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature

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Structure of the apo form of Bacillus stearothermophilus phosphofructokinase.

Mosser Rockann R Reddy Manchi C M MC Bruning John B JB Sacchettini James C JC Reinhart Gregory D GD

Biochemistry 20120111 3

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 i ...[more]

PMID: 22212099

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

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