9x1i: Difference between revisions
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==Structure of endo-beta-N-acetylglucosaminidase HS== | |||
<StructureSection load='9x1i' size='340' side='right'caption='[[9x1i]], [[Resolution|resolution]] 1.81Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9x1i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_oral_metagenome Human oral metagenome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9X1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9X1I 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]] 1.81Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9x1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9x1i OCA], [https://pdbe.org/9x1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9x1i RCSB], [https://www.ebi.ac.uk/pdbsum/9x1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9x1i ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of endo-beta-N-acetylglucosaminidase HSalpha (Endo HSalpha) was determined at 1.8 A resolution, revealing that the enzyme is composed of five distinct domains. Domains I to III adopt a fold that is conserved among GH85 enzymes, with catalytic residues Asn216, Glu218 and Tyr252 corresponding to conserved positions, while Tyr282 is newly implicated in catalysis based on the Endo HSalpha structure. A long loop unique to Endo HSalpha constricts the active site in domain I. Domain IV represents a novel structural element that is not observed in other GH85 enzymes. Its glycan-binding model and structural similarity to known sugar-binding domains play a role in substrate recognition. The minimal contacts with other domains allow it to remain flexible, accommodating bulky substrates at the active site. These features provide insights into the structural basis for substrate specificity and expand the structural diversity of the GH85 family. | |||
Crystal structure of endo-beta-N-acetylglucosaminidase HSalpha.,Kurauchi I, Okura K, Hosokawa C, Ito K, Miyahara I Acta Crystallogr F Struct Biol Commun. 2026 Mar 1;82(Pt 3):94-100. doi: , 10.1107/S2053230X26001214. Epub 2026 Feb 28. PMID:41784007<ref>PMID:41784007</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9x1i" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human oral metagenome]] | |||
[[Category: Large Structures]] | |||
[[Category: Hosokawa C]] | |||
[[Category: Ito K]] | |||
[[Category: Kurauchi I]] | |||
[[Category: Miyahra I]] | |||
[[Category: Okura K]] | |||
Latest revision as of 07:49, 19 March 2026
Structure of endo-beta-N-acetylglucosaminidase HS
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