View source for 6bia


==Crystal structure of Ps i-CgsB==
<StructureSection load='6bia' size='340' side='right'caption='[[6bia]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6bia]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_fuliginea Pseudoalteromonas fuliginea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BIA 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]] 2.8&#8491;</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=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=6bia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bia OCA], [https://pdbe.org/6bia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bia RCSB], [https://www.ebi.ac.uk/pdbsum/6bia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bia ProSAT]</span></td></tr>
</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bia" style="background-color:#fffaf0;"></div>

==See Also==
*[[Sulfatase 3D structures|Sulfatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudoalteromonas fuliginea]]
[[Category: Boraston AB]]
[[Category: Hettle AG]]