6rzd: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
 
Line 3: Line 3:
<StructureSection load='6rzd' size='340' side='right'caption='[[6rzd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='6rzd' size='340' side='right'caption='[[6rzd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6rzd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RZD FirstGlance]. <br>
<table><tr><td colspan='2'>[[6rzd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium_pG7 Uncultured bacterium pG7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RZD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr>
</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&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></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=6rzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rzd OCA], [http://pdbe.org/6rzd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rzd RCSB], [http://www.ebi.ac.uk/pdbsum/6rzd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rzd ProSAT]</span></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=6rzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rzd OCA], [https://pdbe.org/6rzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rzd RCSB], [https://www.ebi.ac.uk/pdbsum/6rzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rzd ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sialic acids are a family of related sugars that play essential roles in many biological events intimately linked to cellular recognition in both health and disease. Sialidases are therefore orchestrators of cellular biology and important therapeutic targets for viral infection. Here, we sought to define if uncharacterized sialidases would provide distinct paradigms in sialic acid biochemistry. We show that a recently discovered sialidase family, whose first member EnvSia156 was isolated from hot spring metagenomes, defines an unusual structural fold and active centre constellation, not previously described in sialidases. Consistent with an inverting mechanism, EnvSia156 reveals a His/Asp active center in which the His acts as a Bronsted acid and Asp as a Bronsted base in a single-displacement mechanism. A predominantly hydrophobic aglycone site facilitates accommodation of a variety of 2-linked sialosides; a versatility that offers the potential for glycan hydrolysis across a range of biological and technological platforms.
Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action.,Bule P, Chuzel L, Blagova E, Wu L, Gray MA, Henrissat B, Rapp E, Bertozzi CR, Taron CH, Davies GJ Nat Commun. 2019 Oct 23;10(1):4816. doi: 10.1038/s41467-019-12684-7. PMID:31645552<ref>PMID:31645552</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rzd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Exo-alpha-sialidase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Blagova, E]]
[[Category: Uncultured bacterium pG7]]
[[Category: Bule, P]]
[[Category: Blagova E]]
[[Category: Chuzel, L]]
[[Category: Bule P]]
[[Category: Davies, G J]]
[[Category: Chuzel L]]
[[Category: Taron, C H]]
[[Category: Davies GJ]]
[[Category: Homodimer]]
[[Category: Taron CH]]
[[Category: Hydrolase]]
[[Category: Inverting]]
[[Category: Sialidase]]
Retrieved from "https://proteopedia.org/6rzd"