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==Crystal structure of Ps i-CgsB C78S in complex with i-neocarratetraose== | ==Crystal structure of Ps i-CgsB C78S in complex with i-neocarratetraose== | ||
<StructureSection load='6b1v' size='340' side='right' caption='[[6b1v]], [[Resolution|resolution]] 2.84Å' scene=''> | <StructureSection load='6b1v' size='340' side='right'caption='[[6b1v]], [[Resolution|resolution]] 2.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6b1v]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B1V OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6b1v]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas Pseudoalteromonas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B1V FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DGS:3,6-ANHYDRO-D-GALACTOSE-2-SULFATE'>DGS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=G4S:4-O-SULFO-BETA-D-GALACTOPYRANOSE'>G4S</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.84Å</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=DGS:3,6-ANHYDRO-D-GALACTOSE-2-SULFATE'>DGS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=G4S:4-O-SULFO-BETA-D-GALACTOPYRANOSE'>G4S</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6b1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b1v OCA], [https://pdbe.org/6b1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b1v RCSB], [https://www.ebi.ac.uk/pdbsum/6b1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b1v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sulfatases play a biologically important role by cleaving sulfate groups from molecules. They can be identified on the basis of signature sequences within their primary structures, and the largest family, S1, has predictable features that contribute specifically to the recognition and catalytic removal of sulfate groups. However, despite advances in the prediction and understanding of S1 sulfatases, a major question regards the molecular determinants that drive substrate recognition beyond the targeted sulfate group. Here, through analysis of an endo-4S-iota-carrageenan sulfatase (PsS1_19A) from Pseudoalteromonas sp. PS47, particularly X-ray crystal structures in complex with intact substrates, we show that specific recognition of the substrate leaving group components, in this case carbohydrate, provides the enzyme with specificity for its substrate. On the basis of these results we propose a catalytic subsite nomenclature that we anticipate will form a general foundation for understanding and describing the molecular basis of substrate recognition by sulfatases. | |||
The Molecular Basis of Polysaccharide Sulfatase Activity and a Nomenclature for Catalytic Subsites in this Class of Enzyme.,Hettle AG, Vickers C, Robb CS, Liu F, Withers SG, Hehemann JH, Boraston AB Structure. 2018 May 1;26(5):747-758.e4. doi: 10.1016/j.str.2018.03.012. Epub 2018, Apr 19. PMID:29681469<ref>PMID:29681469</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6b1v" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sulfatase 3D structures|Sulfatase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudoalteromonas]] | ||
[[Category: | [[Category: Boraston AB]] | ||
[[Category: | [[Category: Hettle AG]] | ||
Latest revision as of 17:30, 4 October 2023
Crystal structure of Ps i-CgsB C78S in complex with i-neocarratetraoseCrystal structure of Ps i-CgsB C78S in complex with i-neocarratetraose
Structural highlights
Publication Abstract from PubMedSulfatases play a biologically important role by cleaving sulfate groups from molecules. They can be identified on the basis of signature sequences within their primary structures, and the largest family, S1, has predictable features that contribute specifically to the recognition and catalytic removal of sulfate groups. However, despite advances in the prediction and understanding of S1 sulfatases, a major question regards the molecular determinants that drive substrate recognition beyond the targeted sulfate group. Here, through analysis of an endo-4S-iota-carrageenan sulfatase (PsS1_19A) from Pseudoalteromonas sp. PS47, particularly X-ray crystal structures in complex with intact substrates, we show that specific recognition of the substrate leaving group components, in this case carbohydrate, provides the enzyme with specificity for its substrate. On the basis of these results we propose a catalytic subsite nomenclature that we anticipate will form a general foundation for understanding and describing the molecular basis of substrate recognition by sulfatases. The Molecular Basis of Polysaccharide Sulfatase Activity and a Nomenclature for Catalytic Subsites in this Class of Enzyme.,Hettle AG, Vickers C, Robb CS, Liu F, Withers SG, Hehemann JH, Boraston AB Structure. 2018 May 1;26(5):747-758.e4. doi: 10.1016/j.str.2018.03.012. Epub 2018, Apr 19. PMID:29681469[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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