7stu: Difference between revisions
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==Crystal structure of sulfatase from Pedobacter yulinensis== | |||
<StructureSection load='7stu' size='340' side='right'caption='[[7stu]], [[Resolution|resolution]] 2.23Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7STU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7STU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DDZ:3,3-DIHYDROXY+L-ALANINE'>DDZ</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7stu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7stu OCA], [https://pdbe.org/7stu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7stu RCSB], [https://www.ebi.ac.uk/pdbsum/7stu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7stu ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:35011319</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7stu" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Sulfatase 3D structures|Sulfatase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Chruszcz M]] | |||
[[Category: Grimes LL]] | |||
[[Category: Lee AL]] | |||
[[Category: O'Malley A]] | |||
[[Category: Schlachter CR]] | |||
[[Category: Tomashek JJ]] | |||
Latest revision as of 14:40, 30 October 2024
Crystal structure of sulfatase from Pedobacter yulinensisCrystal structure of sulfatase from Pedobacter yulinensis
Structural highlights
Publication Abstract from PubMedSulfatases 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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