2lzj

Refined solution structure and dynamics of First Catalytic Cysteine Half-domain from mouse E1 enzyme

spinqualitylabelsall models 2lzj Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2lzj is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UBA1_MOUSE Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP. Publication Abstract from PubMed We report a high resolution NMR structure and 15N relaxation studies of the first catalytic cysteine half-domain (FCCH) of the mouse ubiquitin-activating enzyme E1, together with interaction studies of FCCH and the other catalytic E1 subdomain - SCCH (second catalytic cysteine half-domain). In solution, mouse FCCH forms a well-defined six-stranded antiparallel beta-barrel structure, a common fold for many proteins with a variety of cellular functions. 15N relaxation data reveal FCCH complex backbone dynamics and indicate which residues experience slow intramolecular motions. Some of these residues make contacts with the polar face of ubiquitin in the co-crystal structure of yeast E1 and ubiquitin. However, the titration of FCCH with ubiquitin does not show any visible chemical shift changes in the 2D 1H/15N HSQC spectra of the FCCH. The 2D 1H/15N HSQC experiments performed both for each catalytic half-domain individually and for their equimolar mixture in the milimolar concentration range display no detectable chemical shift perturbation, suggesting a lack of interaction between the two subdomains unless they are covalently linked via the adenylation domain. NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme.,Jaremko M, Jaremko L, Nowakowski M, Wojciechowski M, Szczepanowski RH, Panecka R, Zhukov I, Bochtler M, Ejchart A J Struct Biol. 2013 Nov 6. pii: S1047-8477(13)00299-2. doi:, 10.1016/j.jsb.2013.10.020. PMID:24211821 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 3D structures of Ubiquitin activating enzyme

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