5fre: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Characterization of a novel CBM from Clostridium perfringens== | |||
<StructureSection load='5fre' size='340' side='right' caption='[[5fre]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fre]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FRE FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fra|5fra]]</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=5fre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fre OCA], [http://pdbe.org/5fre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fre RCSB], [http://www.ebi.ac.uk/pdbsum/5fre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fre ProSAT]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5fre" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Imberty, A]] | |||
[[Category: Mahal, L K]] | |||
[[Category: Pau, W]] | [[Category: Pau, W]] | ||
[[Category: | [[Category: Pifferi, C]] | ||
[[Category: Renaudet, O]] | [[Category: Renaudet, O]] | ||
[[Category: Ribeiro, J]] | [[Category: Ribeiro, J]] | ||
[[Category: Varrot, A]] | |||
[[Category: Cbm40]] | |||
[[Category: Hydrolase]] | |||
Revision as of 18:21, 26 July 2016
Characterization of a novel CBM from Clostridium perfringensCharacterization of a novel CBM from Clostridium perfringens
Structural highlights
Publication Abstract from PubMedCBMs (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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||