View source for 6ljl


==Crystal Structure of exoHep-Y390A/H555A complexed with a tetrasaccharide substrate==
<StructureSection load='6ljl' size='340' side='right'caption='[[6ljl]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ljl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_intestinalis_DSM_17393 Bacteroides intestinalis DSM 17393]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LJL 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]] 1.73&#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=GCD:4,5-DEHYDRO-D-GLUCURONIC+ACID'>GCD</scene>, <scene name='pdbligand=IDS:2-O-SULFO-ALPHA-L-IDOPYRANURONIC+ACID'>IDS</scene>, <scene name='pdbligand=SGN:N,O6-DISULFO-GLUCOSAMINE'>SGN</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=6ljl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ljl OCA], [https://pdbe.org/6ljl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ljl RCSB], [https://www.ebi.ac.uk/pdbsum/6ljl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ljl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B3C5J6_9BACE B3C5J6_9BACE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Heparinases (Hepases) are critical tools for the studies of highly heterogeneous heparin (HP)/heparan sulfate (HS). However, exolytic heparinases urgently needed for the sequencing of HP/HS chains remain undiscovered. Herein, a type of exolytic heparinases (exoHepases) is identified from the genomes of different bacteria. These exoHepases share almost no homology with known Hepases and prefer to digest HP rather than HS chains by sequentially releasing unsaturated disaccharides from their reducing ends. The structural study of an exoHepase (BIexoHep) shows that an N-terminal conserved DUF4962 superfamily domain is essential to the enzyme activities of these exoHepases, which is involved in the formation of a unique L-shaped catalytic cavity controlling the sequential digestion of substrates through electrostatic interactions. Further, several HP octasaccharides have been preliminarily sequenced by using BIexoHep. Overall, this study fills the research gap of exoHepases and provides urgently needed tools for the structural and functional studies of HP/HS chains.

Discovery of exolytic heparinases and their catalytic mechanism and potential application.,Zhang Q, Cao HY, Wei L, Lu D, Du M, Yuan M, Shi D, Chen X, Wang P, Chen XL, Chi L, Zhang YZ, Li F Nat Commun. 2021 Feb 24;12(1):1263. doi: 10.1038/s41467-021-21441-8. PMID:33627653<ref>PMID:33627653</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ljl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteroides intestinalis DSM 17393]]
[[Category: Large Structures]]
[[Category: Cao HY]]
[[Category: Li FC]]
[[Category: Wei L]]
[[Category: Zhang QD]]
[[Category: Zhang YZ]]