5XZA

Crystal Structure of Phosphofructokinase from Staphylococcus aureus in complex with ADP

5XZA の概要

• エントリーDOI: 10.2210/pdb5xza/pdb
• 分子名称: ATP-dependent 6-phosphofructokinase, ADENOSINE-5'-DIPHOSPHATE, CITRATE ANION, ... (5 entities in total)
• 機能のキーワード: phosphofructokinase, staphylococcus aureus, transferase
• 由来する生物種: Staphylococcus aureus (strain NCTC 8325)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36663.12

構造登録者

Wang, C.L.,Tian, T.,Zang, J.Y. (登録日: 2017-07-12, 公開日: 2019-03-13, 最終更新日: 2023-11-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)