5fre

Characterization of a novel CBM from Clostridium perfringensCharacterization of a novel CBM from Clostridium perfringens

Structural highlights 5fre is a 3 chain structure with sequence from Clostridium perfringens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: , , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2YQR1_CLOP1 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 5fre, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image