View source for 7pzg


==Phocaeicola vulgatus sialic acid esterase at 1.44 Angstrom resolution==
<StructureSection load='7pzg' size='340' side='right'caption='[[7pzg]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7pzg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Phocaeicola_vulgatus Phocaeicola vulgatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PZG 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]] 1.44&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</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=7pzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pzg OCA], [https://pdbe.org/7pzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pzg RCSB], [https://www.ebi.ac.uk/pdbsum/7pzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pzg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A174J845_PHOVU A0A174J845_PHOVU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sialic acids terminate many N- and O-glycans and are widely distributed on cell surfaces. There are a diverse range of enzymes which interact with these sugars throughout the tree of life. They can act as receptors for influenza and specific betacoronaviruses in viral binding and their cleavage is important in virion release. Sialic acids are also exploited by both commensal and pathogenic bacteria for nutrient acquisition. A common modification of sialic acid is 9-O-acetylation, which can limit the action of sialidases. Some bacteria, including human endosymbionts, employ esterases to overcome this modification. However, few bacterial sialic acid 9-O-acetylesterases (9-O-SAEs) have been structurally characterized. Here, the crystal structure of a 9-O-SAE from Phocaeicola vulgatus (PvSAE) is reported. The structure of PvSAE was determined to resolutions of 1.44 and 2.06 A using crystals from two different crystallization conditions. Structural characterization revealed PvSAE to be a dimer with an SGNH fold, named after the conserved sequence motif of this family, and a Ser-His-Asp catalytic triad. These structures also reveal flexibility in the most N-terminal alpha-helix, which provides a barrier to active-site accessibility. Biochemical assays also show that PvSAE deacetylates both mucin and the acetylated chromophore para-nitrophenyl acetate. This structural and biochemical characterization of PvSAE furthers the understanding of 9-O-SAEs and may aid in the discovery of small molecules targeting this class of enzyme.

The structure of Phocaeicola vulgatus sialic acid acetylesterase.,Scott H, Davies GJ, Armstrong Z Acta Crystallogr D Struct Biol. 2022 May 1;78(Pt 5):647-657. doi:, 10.1107/S2059798322003357. Epub 2022 Apr 26. PMID:35503212<ref>PMID:35503212</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7pzg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Phocaeicola vulgatus]]
[[Category: Armstrong Z]]
[[Category: Davies GJ]]
[[Category: Scott H]]