View source for 7o78


==Structure of the PL6 family chondroitinase B from Pseudopedobacter saltans, Pedsa3807==
<StructureSection load='7o78' size='340' side='right'caption='[[7o78]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7o78]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudopedobacter_saltans_DSM_12145 Pseudopedobacter saltans DSM 12145]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O78 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]] 1.58&#8491;</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=7o78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o78 OCA], [https://pdbe.org/7o78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o78 RCSB], [https://www.ebi.ac.uk/pdbsum/7o78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o78 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F0S763_PSESL F0S763_PSESL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Polysaccharide Lyase Family 6 (PL6) represents one of the 41 polysaccharide lyase families classified in the CAZy database with the vast majority of its members being alginate lyases grouped into three subfamilies, PL6_1-3. To decipher the mode of recognition and action of the enzymes belonging to subfamily PL6_1, we solved the crystal structures of Pedsa0632, Patl3640, Pedsa3628 and Pedsa3807, which all show different substrate specificities and mode of action (endo-/exo-lyase). Thorough exploration of the structures of Pedsa0632 and Patl3640 in complex with their substrates as well as docking experiments confirm that the conserved residues in subsites -1 to +3 of the catalytic site form a common platform which can accommodate various types of alginate in a very similar manner but with a series of original adaptations bringing them their specificities of action. From comparative studies with existing structures of PL6_1 alginate lyases, we observe that in the right-handed parallel beta-helix fold shared by all these enzymes, the substrate binding site harbors the same overall conserved structures and organization. Despite this apparent similarity, it appears that members of the PL6_1 subfamily specifically accommodate and catalyze the degradation of different alginates suggesting that this common platform is actually a highly adaptable and specific tool.

Exploring molecular determinants of polysaccharide Lyase family 6-1 enzyme activity.,Violot S, Galisson F, Carrique L, Jugnarain V, Conchou L, Robert X, Thureau A, Helbert W, Aghajari N, Ballut L Glycobiology. 2021 Jul 10. pii: 6318796. doi: 10.1093/glycob/cwab073. PMID:34245266<ref>PMID:34245266</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7o78" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudopedobacter saltans DSM 12145]]
[[Category: Aghajari N]]
[[Category: Ballut L]]
[[Category: Carrique L]]
[[Category: Violot S]]