5XZ8

Crystal Structure of Phosphofructokinase from Staphylococcus aureus in complex with adenylylimidodiphosphate (the ATP analog) and fructose-6-phosphate

Summary for 5XZ8

• Entry DOI: 10.2210/pdb5xz8/pdb
• Descriptor: ATP-dependent 6-phosphofructokinase, 6-O-phosphono-beta-D-fructofuranose, GLYCEROL, ... (6 entities in total)
• Functional Keywords: phosphofructokinase, staphylococcus aureus, fructose-6-phosphate, transferase
• Biological source: Staphylococcus aureus (strain NCTC 8325)
• Total number of polymer chains: 1
• Total formula weight: 37021.65

Authors

Wang, C.L.,Tian, T.,Zang, J.Y. (deposition date: 2017-07-11, release date: 2019-02-27, Last modification date: 2023-11-22)

Primary citation

Tian, T.,Wang, C.L.,Wu, M.H.,Zhang, X.,Zang, J.Y.
Structural Insights into the Regulation of Staphylococcus aureus Phosphofructokinase by Tetramer-Dimer Conversion.
Biochemistry, 57:4252-4262, 2018

PubMed Abstract: Most reported bacterial phosphofructokinases (Pfks) are tetramers that exhibit activity allosterically regulated via conformational changes between the R and T states. We report that the Pfk from Staphylococcus aureus NCTC 8325 ( SaPfk) exists as both an active tetramer and an inactive dimer in solution. Multiple effectors, including pH, ADP, ATP, and adenylyl-imidodiphosphate (AMP-PNP), cause equilibrium shifts from the tetramer to dimer, whereas the substrate F6P stabilizes SaPfk tetrameric assembly. Crystal structures of SaPfk in complex with different ligands and biochemical analysis reveal that the flexibility of the Gly150-Leu151 motif in helix α7 plays a role in tetramer-dimer conversion. Thus, we propose a molecular mechanism for allosteric regulation of bacterial Pfk via conversion between the tetramer and dimer in addition to the well-characterized R-state/T-state mechanism.

PubMed: 29940104
DOI: 10.1021/acs.biochem.8b00028

Experimental method

X-RAY DIFFRACTION (1.95 Å)