1jfv

X-Ray Structure of oxidised C10S, C15A arsenate reductase from pI258

spinqualitylabelsall models 1jfv, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1jfv is a 1 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: K, LCP, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ARSC_STAAU Reduces arsenate [As(V)] to arsenite [As(III)] and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Could switch between different functions in different circumstances.[HAMAP-Rule:MF_01624] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Arsenate reductase (ArsC) from Staphylococcus aureus plasmid pI258 plays a role in bacterial heavy metal resistance and catalyzes the reduction of arsenate to arsenite. The structures of the oxidized and reduced forms of ArsC were solved. ArsC has the PTPase I fold typical for low molecular weight tyrosine phosphatases (LMW PTPases). Remarkably, kinetic experiments show that pI258 ArsC also catalyzes the tyrosine phosphatase reaction in addition to arsenate reduction. These results provide evidence that ArsC from pI258 evolved from LMW PTPase by the grafting of a redox function onto a pre-existing catalytic site and that its evolutionary origin is different from those of arsenate reductases from Escherichia coli plasmid R773 and from Saccharomyces cerevisiae. The mechanism proposed here for the catalysis of arsenate reduction by pI258 ArsC involves a nucleophilic attack by Cys 10 on arsenate, the formation of a covalent intermediate and the transport of oxidative equivalents by a disulfide cascade. The reaction is associated with major structural changes in the ArsC. Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty.,Zegers I, Martins JC, Willem R, Wyns L, Messens J Nat Struct Biol. 2001 Oct;8(10):843-7. PMID:11573087 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Arsenate reductase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA