A complex iron-calcium cofactor catalyzing phosphotransfer chemistry.
A complex iron-calcium cofactor catalyzing phosphotransfer chemistry.
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DOI:
10.1126/science.1254237
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发表时间:
2014-09-05
期刊:
影响因子:
--
通讯作者:
Berks BC
中科院分区:
文献类型:
--
作者:
Yong SC;Roversi P;Lillington J;Rodriguez F;Krehenbrink M;Zeldin OB;Garman EF;Lea SM;Berks BC
Alkaline phosphatases play a crucial role in phosphate acquisition by microorganisms. To expand our understanding of catalysis by this class of enzymes we have determined the structure of the widely-occurring microbial alkaline phosphatase PhoX. The enzyme contains a complex active site cofactor comprising two antiferromagnetically-coupled Fe3+ ions, three Ca2+ ions, and a μ3-bridging oxo group. Notably, the main part of the cofactor resembles synthetic oxide-centered triangular metal complexes. Structures of PhoX-ligand complexes reveal how the active site metal ions bind substrate and implicate the cofactor oxo group in the catalytic mechanism. The presence of iron in PhoX raises the possibility that iron bioavailability limits microbial phosphate acquisition.
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