Evidence map›Paper›PMID 21865160›Full record

ArticleThe Journal of biological chemistry2011

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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Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

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0cells of the map it votes in
4citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. ApaH decaps NpNature chemical biology · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Yong-Liang JiangHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
Jun-Wei ZhangHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
Wei-Li YuHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
Wang ChengHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
Chen-Chen ZhangHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China.
Cecile FroletLaboratoire d'Ingénierie des Macromolécules, Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble, France.
Anne-Marie Di GuilmiLaboratoire d'Ingénierie des Macromolécules, Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble, France.
Thierry VernetLaboratoire d'Ingénierie des Macromolécules, Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble, France.
Cong-Zhao ZhouHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China. Electronic address: zcz@ustc.edu.cn.
Yuxing ChenHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China. Electronic address: cyxing@ustc.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Protein FoldingAcid Anhydride HydrolasesAdenosine TriphosphatasesApoenzymesBacterial ProteinsBinding SitesCrystallography, X-RayProtein Structure, SecondaryStreptococcus pneumoniaeAcid Anhydride HydrolasesAdenosine TriphosphatasesApoenzymesBacterial Proteinsdiadenosine polyphosphate hydrolase

Identifiers

PMID21865160
PMCPMC3195627

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