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Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene.

ABSTRACT: Escherichia coli YfcE belongs to a conserved protein family within the calcineurin-like phosphoesterase superfamily (Pfam00149) that is widely distributed in bacteria and archaea. Superfamily members are metallophosphatases that include monoesterases and diesterases involved in a variety of cellular functions. YfcE exhibited catalytic activity against bis-p-nitrophenyl phosphate, a general substrate for phosphodiesterases, and had an absolute requirement for Mn2+. However, no activity was observed with phosphodiesters and over 50 naturally occurring phosphomonoesters. The crystal structure of the YfcE phosphodiesterase has been determined to 2.25 A resolution. YfcE has a beta-sandwich architecture similar to metallophosphatases of common ancestral origin. Unlike its more complex homologs that have added structural elements for regulation and substrate recognition, the relatively small 184-amino-acid protein has retained its ancestral simplicity. The tetrameric protein carries two zinc ions per active site from the E. coli extract that reflect the conserved di-Mn2+ active site geometry. A cocrystallized sulfate inhibitor mimics the binding of phosphate moeities in known ligand/phosphatase complexes. Thus, YfcE has a similar active site and biochemical mechanism as well-characterized superfamily members, while the YfcE phosphodiester-containing substrate is unique.

SUBMITTER: Miller DJ

PROVIDER: S-EPMC2206680 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature

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Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene.

Miller Darcie J DJ Shuvalova Ludmilla L Evdokimova Elena E Savchenko Alexei A Yakunin Alexander F AF Anderson Wayne F WF

Protein science : a publication of the Protein Society 20070701 7

Escherichia coli YfcE belongs to a conserved protein family within the calcineurin-like phosphoesterase superfamily (Pfam00149) that is widely distributed in bacteria and archaea. Superfamily members are metallophosphatases that include monoesterases and diesterases involved in a variety of cellular functions. YfcE exhibited catalytic activity against bis-p-nitrophenyl phosphate, a general substrate for phosphodiesterases, and had an absolute requirement for Mn2+. However, no activity was observ ...[more]

PMID: 17586769

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Dataset Information

Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene.

Publications

Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene.

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