Chen-Chen Zhang

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Publications (2)9.55 Total impact

  • Article: Structural and Enzymatic Characterization of the Streptococcal ATP/Diadenosine Polyphosphate and Phosphodiester Hydrolase Spr1479/SapH
    Yong-Liang Jiang, Jun-Wei Zhang, Wei-Li Yu, Wang Cheng, Chen-Chen Zhang, Cecile Frolet, Anne-Marie Di Guilmi, Thierry Vernet, Cong-Zhao Zhou, Yuxing Chen
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    ABSTRACT: Spr1479 from Streptococcus pneumoniae R6 is a 33-kDa hypothetical protein of unknown function. Here, we determined the crystal structures of its apo-form at 1.90 Å and complex forms with inorganic phosphate and AMP at 2.30 and 2.20 Å, respectively. The core structure of Spr1479 adopts a four-layer αββα-sandwich fold, with Fe3+ and Mn2+ coordinated at the binuclear center of the active site (similar to metallophosphoesterases). Enzymatic assays showed that, in addition to phosphodiesterase activity for bis(p-nitrophenyl) phosphate, Spr1479 has hydrolase activity for diadenosine polyphosphate (ApnA) and ATP. Residues that coordinate with the two metals are indispensable for both activities. By contrast, the streptococcus-specific residue Trp-67, which binds to phosphate in the two complex structures, is indispensable for the ATP/ApnA hydrolase activity only. Moreover, the AMP-binding pocket is conserved exclusively in all streptococci. Therefore, we named the protein SapH for streptococcal ATP/ApnA and phosphodiester hydrolase.
    Journal of Biological Chemistry 10/2011; 286(41):35906-35914. · 4.77 Impact Factor
  • Article: Structural and enzymatic characterization of the streptococcal ATP/diadenosine polyphosphate and phosphodiester hydrolase Spr1479/SapH.
    Yong-Liang Jiang, Jun-Wei Zhang, Wei-Li Yu, Wang Cheng, Chen-Chen Zhang, Cecile Frolet, Anne-Marie Di Guilmi, Thierry Vernet, Cong-Zhao Zhou, Yuxing Chen
    [show abstract] [hide abstract]
    ABSTRACT: Spr1479 from Streptococcus pneumoniae R6 is a 33-kDa hypothetical protein of unknown function. Here, we determined the crystal structures of its apo-form at 1.90 Å and complex forms with inorganic phosphate and AMP at 2.30 and 2.20 Å, respectively. The core structure of Spr1479 adopts a four-layer αββα-sandwich fold, with Fe(3+) and Mn(2+) coordinated at the binuclear center of the active site (similar to metallophosphoesterases). Enzymatic assays showed that, in addition to phosphodiesterase activity for bis(p-nitrophenyl) phosphate, Spr1479 has hydrolase activity for diadenosine polyphosphate (Ap(n)A) and ATP. Residues that coordinate with the two metals are indispensable for both activities. By contrast, the streptococcus-specific residue Trp-67, which binds to phosphate in the two complex structures, is indispensable for the ATP/Ap(n)A hydrolase activity only. Moreover, the AMP-binding pocket is conserved exclusively in all streptococci. Therefore, we named the protein SapH for streptococcal ATP/Ap(n)A and phosphodiester hydrolase.
    Journal of Biological Chemistry 08/2011; 286(41):35906-14. · 4.77 Impact Factor
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