2PK0

Structure of the S. agalactiae serine/threonine phosphatase at 2.65 resolution

2PK0 の概要

• エントリーDOI: 10.2210/pdb2pk0/pdb
• 分子名称: Serine/threonine protein phosphatase Stp1, MAGNESIUM ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: streptococcus agalactiae, serine, threonine, phosphatase, signaling motif, signaling protein
• 由来する生物種: Streptococcus agalactiae
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 109988.38

構造登録者

Rantanen, M.K.,Lehtio, L.,Rajagopal, L.,Rubens, C.E.,Goldman, A. (登録日: 2007-04-17, 公開日: 2007-06-12, 最終更新日: 2024-04-03)

主引用文献

Rantanen, M.K.,Lehtio, L.,Rajagopal, L.,Rubens, C.E.,Goldman, A.
Structure of Streptococcus agalactiae serine/threonine phosphatase. The subdomain conformation is coupled to the binding of a third metal ion
Febs J., 274:3128-3137, 2007

PubMed Abstract: We solved the crystal structure of Streptococcus agalactiae serine/threonine phosphatase (SaSTP) using a combination of single-wavelength anomalous dispersion phasing and molecular replacement. The overall structure resembles that of previously characterized members of the PPM/PP2C STP family. The asymmetric unit contains four monomers and we observed two novel conformations for the flap domain among them. In one of these conformations, the enzyme binds three metal ions, whereas in the other it binds only two. The three-metal ion structure also has the active site arginine in a novel conformation. The switch between the two- and three-metal ion structures appears to be binding of another monomer to the active site of STP, which promotes binding of the third metal ion. This interaction may mimic the binding of a product complex, especially since the motif binding to the active site contains a serine residue aligning remarkably well with the phosphate found in the human STP structure.

PubMed: 17521332
DOI: 10.1111/j.1742-4658.2007.05845.x

実験手法

X-RAY DIFFRACTION (2.65 Å)