View source for 5fra


==CBM40_CPF0721-6'SL==
<StructureSection load='5fra' size='340' side='right'caption='[[5fra]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fra]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FRA 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]] 2&#8491;</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=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</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=5fra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fra OCA], [https://pdbe.org/5fra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fra RCSB], [https://www.ebi.ac.uk/pdbsum/5fra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fra ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H2YQR1_CLOP1 A0A0H2YQR1_CLOP1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CBMs (carbohydrate-binding modules) are a class of polypeptides usually associated with carbohydrate-active enzymatic sites. We have characterized a new member of the CBM40 family, coded from a section of the gene NanI from Clostridium perfringens Glycan arrays revealed its preference towards alpha(2,3)-linked sialosides, which was confirmed and quantified by calorimetric studies. The CBM40 binds to alpha(2,3)-sialyl-lactose with a Kd of approximately 30 muM, the highest affinity value for this class of proteins. Inspired by lectins' structure and their arrangement as multimeric proteins, we have engineered a dimeric form of the CBM, and using SPR (surface plasmon resonance) we have observed 6-11-fold binding increases due to the avidity affect. The structures of the CBM, resolved by X-ray crystallography, in complex with alpha(2,3)- or alpha(2,6)-sialyl-lactose explain its binding specificity and unusually strong binding.

Characterization of a high-affinity sialic acid-specific CBM40 from Clostridium perfringens and engineering of a divalent form.,Ribeiro JP, Pau W, Pifferi C, Renaudet O, Varrot A, Mahal LK, Imberty A Biochem J. 2016 Jul 15;473(14):2109-18. doi: 10.1042/BCJ20160340. Epub 2016 May, 17. PMID:27208171<ref>PMID:27208171</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fra" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium perfringens]]
[[Category: Large Structures]]
[[Category: Imberty A]]
[[Category: Mahal LK]]
[[Category: Pau W]]
[[Category: Pifferi C]]
[[Category: Renaudet O]]
[[Category: Ribeiro JP]]
[[Category: Varrot A]]