5tsp

Crystal structure of the catalytic domain of Clostridium perfringens neuraminidase (NanI) in complex with a CHES

spinqualitylabelsall models 5tsp, resolution 1.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tsp is a 2 chain structure with sequence from Clostridium perfringens ATCC 13124. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.24Å Ligands: CA, NHE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2YQR1_CLOP1 Publication Abstract from PubMed Anti-bacterial and anti-viral neuraminidase agents inhibit neuraminidase activity catalyzing the hydrolysis of terminal N-acetylneuraminic acid (Neu5Ac) from glycoconjugates and help to prevent the host pathogenesis that lead to fatal infectious diseases including influenza, bacteremia, sepsis, and cholera. Emerging antibiotic and drug resistances to commonly used anti-neuraminidase agents such as oseltamivir (Tamiflu) and zanamivir (Relenza) have highlighted the need to develop new anti-neuraminidase drugs. We obtained a serendipitous complex crystal of the catalytic domain of Clostridium perfringens neuraminidase (CpNanICD) with 2-(cyclohexylamino)ethanesulfonic acid (CHES) as a buffer. Here, we report the crystal structure of CpNanICD in complex with CHES at 1.24 A resolution. Amphipathic CHES binds to the catalytic site of CpNanICD similar to the substrate (Neu5Ac) binding site. The 2-aminoethanesulfonic acid moiety and cyclohexyl groups of CHES interact with the cluster of three arginine residues and with the hydrophobic pocket of the CpNanICD catalytic site. In addition, a structural comparison with other bacterial and human neuraminidases suggests that CHES could serve as a scaffold for the development of new anti-neuraminidase agents targeting CpNanI. Crystal structure of the catalytic domain of Clostridium perfringens neuraminidase in complex with a non-carbohydrate-based inhibitor, 2-(cyclohexylamino)ethanesulfonic acid.,Lee Y, Youn HS, Lee JG, An JY, Park KR, Kang JY, Ryu YB, Jin MS, Park KH, Eom SH Biochem Biophys Res Commun. 2017 Apr 29;486(2):470-475. doi:, 10.1016/j.bbrc.2017.03.064. Epub 2017 Mar 16. PMID:28315686 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Neuraminidase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA