5DJF

Structure of M. tuberculosis CysQ, a PAP phosphatase - ligand-free structure

5DJF の概要

• エントリーDOI: 10.2210/pdb5djf/pdb
• 関連するPDBエントリー: 5DJG 5DJH 5DJI 5DJJ 5DJK
• 分子名称: 3'-phosphoadenosine 5'-phosphate phosphatase, SODIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: cysq, pap phosphatase, apo-enzyme, hydrolase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30953.77

構造登録者

Erickson, A.I.,Fisher, A.J. (登録日: 2015-09-02, 公開日: 2015-11-11, 最終更新日: 2024-03-06)

主引用文献

Erickson, A.I.,Sarsam, R.D.,Fisher, A.J.
Crystal Structures of Mycobacterium tuberculosis CysQ, with Substrate and Products Bound.
Biochemistry, 54:6830-6841, 2015

PubMed Abstract: In many organisms, 3'-phosphoadenosine 5'-phosphate (PAP) is a product of two reactions in the sulfur activation pathway. The sulfurylation of biomolecules, catalyzed by sulfotransferases, uses 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as a sulfate donor, producing the sulfated biomolecule and PAP product. Additionally, the first step in sulfate reduction for many bacteria and fungi reduces the sulfate moiety of PAPS, producing PAP and sulfite, which is subsequently reduced to sulfide. PAP is removed by the phosphatase activity of CysQ, a 3',5'-bisphosphate nucleotidase, yielding AMP and phosphate. Because excess PAP alters the equilibrium of the sulfur pathway and inhibits sulfotransferases, PAP concentrations can affect the levels of sulfur-containing metabolites. Therefore, CysQ, a divalent cation metal-dependent phosphatase, is a major regulator of this pathway. CysQ (Rv2131c) from Mycobacterium tuberculosis (Mtb) was successfully expressed, purified, and crystallized in a variety of ligand-bound states. Here we report six crystal structures of Mtb CysQ, including a ligand-free structure, a lithium-inhibited state with substrate PAP bound, and a product-bound complex with AMP, phosphate, and three Mg(2+) ions bound. Comparison of these structures together with homologues of the superfamily has provided insight into substrate specificity, metal coordination, and catalytic mechanism.

PubMed: 26512869
DOI: 10.1021/acs.biochem.5b01000

実験手法

X-RAY DIFFRACTION (1.7 Å)