View source for 7dc4


==Crystal structure of glycan-bound Pseudomonas taiwanensis lectin==
<StructureSection load='7dc4' size='340' side='right'caption='[[7dc4]], [[Resolution|resolution]] 0.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7dc4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_taiwanensis_DSM_21245 Pseudomonas taiwanensis DSM 21245]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DC4 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]] 0.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=7dc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dc4 OCA], [https://pdbe.org/7dc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dc4 RCSB], [https://www.ebi.ac.uk/pdbsum/7dc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dc4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2L1HSZ4_9PSED A0A2L1HSZ4_9PSED] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Homologues of the Oscillatoria agardhii agglutinin (OAA) lectins contain a sequence repeat of approximately 66 amino acids, with the number of tandem repeats varying across family members. OAA homologues bind high-mannose glycans on viral surface proteins, thereby interfering with viral entry into host cells. As such, OAA homologues have potential utility as antiviral agents, but a more detailed understanding of their structure-function relationships would enable us to develop improved constructs. Here, we determined the X-ray crystal structure of free and glycan-bound forms of Pseudomonas taiwanensis lectin (PTL), an OAA-family lectin consisting of two tandem repeats. Like other OAA-family lectins, PTL exhibited a beta-barrel-like structure with two symmetrically positioned glycan-binding sites at the opposite ends of the barrel. Upon glycan binding, the conformation of PTL undergoes a more significant change than expected from previous OAA structural analysis. Moreover, the electron density of the bound glycans suggested that the binding affinities are different at the two binding sites. Next, based on analysis of these structures, we used site-specific mutagenesis to create PTL constructs expected to increase the population with a conformation suitable for glycan binding. The engineered PTLs were examined for their antiviral activity against the influenza virus. Interestingly, some exhibited stronger activity compared with that of the parent PTL. We propose that our approach is effective for the generation of potential microbicides with enhanced antiviral activity.

Lectins engineered to favor a glycan-binding conformation have enhanced antiviral activity.,Matoba Y, Sato Y, Oda K, Hatori Y, Morimoto K J Biol Chem. 2021 Apr 22:100698. doi: 10.1016/j.jbc.2021.100698. PMID:33895142<ref>PMID:33895142</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7dc4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas taiwanensis DSM 21245]]
[[Category: Matoba Y]]
[[Category: Oda K]]