6g5z
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6g5z]] 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=6G5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G5Z FirstGlance]. <br> | <table><tr><td colspan='2'>[[6g5z]] 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=6G5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6G5Z FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DDZ:3,3-DIHYDROXY+L-ALANINE'>DDZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DDZ:3,3-DIHYDROXY+L-ALANINE'>DDZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6g5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g5z OCA], [https://pdbe.org/6g5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g5z RCSB], [https://www.ebi.ac.uk/pdbsum/6g5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g5z ProSAT]</span></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=6g5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g5z OCA], [https://pdbe.org/6g5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6g5z RCSB], [https://www.ebi.ac.uk/pdbsum/6g5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6g5z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BETC_RHIME BETC_RHIME] Converts choline-O-sulfate into choline. | [https://www.uniprot.org/uniprot/BETC_RHIME BETC_RHIME] Converts choline-O-sulfate into choline. | ||
| - | <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 6g5z" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Sulfatase 3D structures|Sulfatase 3D structures]] | *[[Sulfatase 3D structures|Sulfatase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:49, 7 February 2024
Choline sulfatase from Ensifer (Sinorhizobium) meliloti
| |||||||||||
