4fnv

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==Crystal Structure of Heparinase III==
==Crystal Structure of Heparinase III==
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<StructureSection load='4fnv' size='340' side='right' caption='[[4fnv]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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<StructureSection load='4fnv' size='340' side='right'caption='[[4fnv]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fnv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron Bacteroides thetaiotaomicron]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FNV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FNV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fnv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FNV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FNV FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fnv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fnv RCSB], [http://www.ebi.ac.uk/pdbsum/4fnv PDBsum]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fnv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fnv OCA], [https://pdbe.org/4fnv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fnv RCSB], [https://www.ebi.ac.uk/pdbsum/4fnv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fnv ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/HEPC_BACTN HEPC_BACTN] Specifically cleaves heparan sulfate-rich regions of acidic polysaccharides. Does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated glucosamine linkages. Functions in cleaving metazoan heparan sulfate and providing carbon, nitrogen and sulfate sources for microorganisms.<ref>PMID:23011846</ref>
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Heparinase III (HepIII) is a 73-kDa polysaccharide lyase (PL) that degrades the heparan sulfate (HS) polysaccharides at sulfate-rare regions, which are important co-factors for a vast array of functional distinct proteins including the well-characterized antithrombin and the FGF/FGFR signal transduction system. It functions in cleaving metazoan heparan sulfate (HS) and providing carbon, nitrogen and sulfate sources for host microorganisms. It has long been used to deduce the structure of HS and heparin motifs; however, the structure of its own is unknown. Here we report the crystal structure of the HepIII from Bacteroides thetaiotaomicron at a resolution of 1.6 A. The overall architecture of HepIII belongs to the (alpha/alpha)5 toroid subclass with an N-terminal toroid-like domain and a C-terminal beta-sandwich domain. Analysis of this high-resolution structure allows us to identify a potential HS substrate binding site in a tunnel between the two domains. A tetrasaccharide substrate bound model suggests an elimination mechanism in the HS degradation. Asn260 and His464 neutralize the carboxylic group, whereas Tyr314 serves both as a general base in C-5 proton abstraction, and a general acid in a proton donation to reconstitute the terminal hydroxyl group, respectively. The structure of HepIII and the proposed reaction model provide a molecular basis for its potential practical utilization and the mechanism of its eliminative degradation for HS polysaccarides.
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Structural basis of heparan sulfate-specific degradation by heparinase III.,Dong W, Lu W, McKeehan WL, Luo Y, Ye S Protein Cell. 2012 Jul 21. PMID:23011846<ref>PMID:23011846</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacteroides thetaiotaomicron]]
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[[Category: Bacteroides thetaiotaomicron VPI-5482]]
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[[Category: Dong, W]]
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[[Category: Large Structures]]
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[[Category: Ye, S]]
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[[Category: Dong W]]
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[[Category: Sandwich fold]]
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[[Category: Ye S]]
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[[Category: Heparan sulfate degradation]]
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[[Category: Lyase]]
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[[Category: Toroid fold]]
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Crystal Structure of Heparinase III

PDB ID 4fnv

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