1rlm
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Crystal Structure of ybiV from Escherichia coli K12
OverviewOverview
The protein YbiV from Escherichia coli K12 MG1655 is a hypothetical, protein with sequence homology to the haloacid dehalogenase (HAD), superfamily of proteins. Although numerous members of this family have, been identified, the functions of few are known. Using the crystal, structure, sequence analysis, and biochemical assays, we have, characterized YbiV as a HAD phosphatase. The crystal structure of YbiV, reveals a two-domain protein, one with the characteristic HAD hydrolase, fold, the other an inserted alpha/beta fold. In an effort to understand, the mechanism, we also solved and report the structures of YbiV in complex, with beryllofluoride (BeF3-) and aluminum trifluoride (AlF3), which have, been shown to mimic the phosphorylated intermediate and transition state, for hydrolysis, respectively, in analogy to other HAD phosphatases., Analysis of the structures reveals the substrate-binding cavity, which is, hydrophilic in nature. Both structure and sequence homology indicate YbiV, may be a sugar phosphatase, which is supported by biochemical assays that, measured the release of free phosphate on a number of sugar-like, substrates. We also investigated available genomic and functional data in, an effort to determine the physiological substrate.
About this StructureAbout this Structure
1RLM is a Single protein structure of sequence from Escherichia coli with MG and GOL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
YbiV from Escherichia coli K12 is a HAD phosphatase., Roberts A, Lee SY, McCullagh E, Silversmith RE, Wemmer DE, Proteins. 2005 Mar 1;58(4):790-801. PMID:15657928
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