3U96

Crystal Structure of YopHQ357F(Catalytic Domain, Residues 163-468) in complex with pNCS

3U96 の概要

• エントリーDOI: 10.2210/pdb3u96/pdb
• 分子名称: Tyrosine-protein phosphatase yopH, N,4-DIHYDROXY-N-OXO-3-(SULFOOXY)BENZENAMINIUM, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: yoph, ptpase, hydrolase
• 由来する生物種: Yersinia enterocolitica
• 細胞内の位置: Secreted: P15273
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67740.16

構造登録者

Ho, M.C.,Ke, S. (登録日: 2011-10-17, 公開日: 2012-08-29, 最終更新日: 2024-03-20)

主引用文献

Ke, S.,Ho, M.C.,Zhadin, N.,Deng, H.,Callender, R.
Investigation of catalytic loop structure, dynamics, and function relationship of Yersinia protein tyrosine phosphatase by temperature-jump relaxation spectroscopy and X-ray structural determination.
J.Phys.Chem.B, 116:6166-6176, 2012

PubMed Abstract: Yersinia protein tyrosine phosphatase (YopH) is the most efficient enzyme among all PTPases. YopH is hyperactive compared to human PTPases, interfering with mammalian cellular pathways to achieve the pathogenicity of Yersinia. Two properties related to the catalytic loop structure differences have been proposed to affect its dynamics and enzyme efficiency. One is the ability of the loop to form stabilizing interactions to bound ligand after loop closure, which has long been recognized. In addition, the loop flexibility/mobility was suggested in a previous study to be a factor as well, based on the observation that incremental changes in PTPase loop structure by single point mutations to alanine often induce incremental changes in enzyme catalytic efficiency. In this study, the temperature jump relaxation spectroscopy (T-jump) has been used to discern the subtle changes of the loop dynamics due to point loop mutations. As expected, our results suggest a correlation between loop dynamics and the size of the residue on the catalytic loop. The stabilization of the enzyme-ligand complex is often enthalpy driven, achieved by formation of additional favorable hydrogen bonding/ionic interactions after loop closure. Interestingly, our T-jump and X-ray crystallography studies on YopH suggest that the elimination of some ligand-protein interactions by mutation does not necessarily destabilize the ligand-enzyme complex after loop closure, since the increased entropy in the forms of more mobile protein residues may be sufficient to compensate the free energy loss due to lost interactions and may even lead to enhanced efficiency of the enzyme catalysis. How these competing loop properties may affect loop dynamics and enzyme function are discussed.

PubMed: 22564106
DOI: 10.1021/jp3037846

実験手法

X-RAY DIFFRACTION (1.8 Å)