7stu

Crystal structure of sulfatase from Pedobacter yulinensis

spinqualitylabelsall models 7stu, resolution 2.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.23Å Ligands: BR, CA, DDZ, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Sulfatases are ubiquitous enzymes that hydrolyze sulfate from sulfated organic substrates such as carbohydrates, steroids, and flavones. These enzymes can be exploited in the field of biotechnology to analyze sulfated metabolites in humans, such as steroids and drugs of abuse. Because genomic data far outstrip biochemical characterization, the analysis of sulfatases from published sequences can lead to the discovery of new and unique activities advantageous for biotechnological applications. We expressed and characterized a putative sulfatase (PyuS) from the bacterium Pedobacter yulinensis. PyuS contains the (C/S)XPXR sulfatase motif, where the Cys or Ser is post-translationally converted into a formylglycine residue (FGly). His-tagged PyuS was co-expressed in Escherichia coli with a formylglycine-generating enzyme (FGE) from Mycobacterium tuberculosis and purified. We obtained several crystal structures of PyuS, and the FGly modification was detected at the active site. The enzyme has sulfatase activity on aromatic sulfated substrates as well as phosphatase activity on some aromatic phosphates; however, PyuS did not have detectable activity on 17alpha-estradiol sulfate, cortisol 21-sulfate, or boldenone sulfate. Purification, Characterization, and Structural Studies of a Sulfatase from Pedobacter yulinensis.,Schlachter CR, O'Malley A, Grimes LL, Tomashek JJ, Chruszcz M, Lee LA Molecules. 2021 Dec 24;27(1). pii: molecules27010087. doi:, 10.3390/molecules27010087. PMID:35011319 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sulfatase 3D structures

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