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7ptj
From Proteopedia
(Difference between revisions)
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==C54S mutant of choline-sulfatase from E. meliloti CECT4857 bound to HEPES== | ==C54S mutant of choline-sulfatase from E. meliloti CECT4857 bound to HEPES== | ||
| - | <StructureSection load='7ptj' size='340' side='right'caption='[[7ptj]]' scene=''> | + | <StructureSection load='7ptj' size='340' side='right'caption='[[7ptj]], [[Resolution|resolution]] 2.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PTJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ptj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PTJ FirstGlance]. <br> |
| - | </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=7ptj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ptj OCA], [https://pdbe.org/7ptj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ptj RCSB], [https://www.ebi.ac.uk/pdbsum/7ptj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ptj ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7ptj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ptj OCA], [https://pdbe.org/7ptj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ptj RCSB], [https://www.ebi.ac.uk/pdbsum/7ptj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ptj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/A0A410NSD4_RHIML A0A410NSD4_RHIML]] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Choline-O-sulfatase (COSe; EC 3.1.6.6) is a member of the alkaline phosphatase (AP) superfamily, and its natural function is to hydrolyze choline-O-sulfate into choline and sulfate. Despite its natural function, the major interest in this enzyme resides in the landmark catalytic/substrate promiscuity of sulfatases, which has led to attention in the biotechnological field due to their potential in protein engineering. In this work, an in-depth structural analysis of wild-type Sinorhizobium (Ensifer) meliloti COSe (SmeCOSe) and its C54S active-site mutant is reported. The binding mode of this AP superfamily member to both products of the reaction (sulfate and choline) and to a substrate-like compound are shown for the first time. The structures further confirm the importance of the C-terminal extension of the enzyme in becoming part of the active site and participating in enzyme activity through dynamic intra-subunit and inter-subunit hydrogen bonds (Asn146(A)-Asp500(B)-Asn498(B)). These residues act as the `gatekeeper' responsible for the open/closed conformations of the enzyme, in addition to assisting in ligand binding through the rearrangement of Leu499 (with a movement of approximately 5 A). Trp129 and His145 clamp the quaternary ammonium moiety of choline and also connect the catalytic cleft to the C-terminus of an adjacent protomer. The structural information reported here contrasts with the proposed role of conformational dynamics in promoting the enzymatic catalytic proficiency of an enzyme. | ||
| + | |||
| + | Structural insights into choline-O-sulfatase reveal the molecular determinants for ligand binding.,Gavira JA, Camara-Artigas A, Neira JL, Torres de Pinedo JM, Sanchez P, Ortega E, Martinez-Rodriguez S Acta Crystallogr D Struct Biol. 2022 May 1;78(Pt 5):669-682. doi:, 10.1107/S2059798322003709. Epub 2022 Apr 26. PMID:35503214<ref>PMID:35503214</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ptj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Sinorhizobium meliloti]] | ||
[[Category: Gavira JA]] | [[Category: Gavira JA]] | ||
[[Category: Martinez-Rodriguez S]] | [[Category: Martinez-Rodriguez S]] | ||
Revision as of 03:11, 8 September 2022
C54S mutant of choline-sulfatase from E. meliloti CECT4857 bound to HEPES
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