View source for 6xaq


==Alpha-methyl-glucose-bound structure of Marinomonas primoryensis PA14 carbohydrate-binding domain==
<StructureSection load='6xaq' size='340' side='right'caption='[[6xaq]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xaq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinomonas_primoryensis Marinomonas primoryensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XAQ 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]] 1.2&#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=GYP:METHYL-ALPHA-D-GLUCOPYRANOSIDE'>GYP</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=6xaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xaq OCA], [https://pdbe.org/6xaq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xaq RCSB], [https://www.ebi.ac.uk/pdbsum/6xaq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xaq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A1YIY3_9GAMM A1YIY3_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Carbohydrate recognition by lectins governs critical host-microbe interactions. MpPA14 (Marinomonas primoryensis PA14 domain) lectin is a domain of a 1.5-MDa adhesin responsible for a symbiotic bacterium-diatom interaction in Antarctica. Here, we show that MpPA14 binds various monosaccharides, with l-fucose and N-acetylglucosamine being the strongest ligands (dissociation constant [Kd ], approximately 150 muM). High-resolution structures of MpPA14 with 15 different sugars bound elucidated the molecular basis for the lectin's apparent binding promiscuity but underlying selectivity. MpPA14 mediates strong Ca(2+)-dependent interactions with the 3,4-diols of l-fucopyranose and glucopyranoses, and it binds other sugars via their specific minor isomers. Thus, MpPA14 only binds polysaccharides like branched glucans and fucoidans with these free end groups. Consistent with our findings, adhesion of MpPA14 to diatom cells was selectively blocked by l-fucose, but not by N-acetyl galactosamine. The MpPA14 lectin homolog present in a Vibrio cholerae adhesin was produced and was shown to have the same sugar binding preferences as MpPA14. The pathogen's lectin was unable to effectively bind the diatom in the presence of fucose, thus demonstrating the antiadhesion strategy of blocking infection via ligand-based antagonists.IMPORTANCE Bacterial adhesins are key virulence factors that are essential for the pathogen-host interaction and biofilm formation that cause most infections. Many of the adhesin-driven cell-cell interactions are mediated by lectins. Our study reveals for the first time the molecular basis underlying the binding selectivity of a common bacterial adhesin lectin from the marine bacterium Marinomonas primoryensis, homologs of which are found in both environmental and pathogenic species. The lectin-ligand interactions illustrated at the atomic level guided the identification of a ligand that serves as an inhibitor to block bacterium-host adhesion. With conventional bactericidal antibiotics losing their potency due to resistance, our work gives critical insight into an antiadhesion strategy to treat bacterial infections.

Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation.,Guo S, Vance TDR, Zahiri H, Eves R, Stevens C, Hehemann JH, Vidal-Melgosa S, Davies PL mBio. 2021 Apr 6;12(2). pii: mBio.00130-21. doi: 10.1128/mBio.00130-21. PMID:33824212<ref>PMID:33824212</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6xaq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Antifreeze protein 3D structures|Antifreeze protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Marinomonas primoryensis]]
[[Category: Davies PL]]
[[Category: Guo S]]