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![[Figure 2]](be5254fig2mag.jpg)
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Figure 2
Simulated-annealing OMIT maps of the adenylated and covalently bound ubiquitin molecules. (a) Simulated-annealing 2Fo − Fc OMIT map contoured at an r.m.s. deviation of 1 (grey mesh) for adenylated ubiquitin, Ub(a) (PDB entry 4nnj, chain D), coloured in yellow. The Uba1 molecule is coloured transparent green. (b) Simulated-annealing 2Fo − Fc OMIT map (grey mesh) of the covalently linked ubiquitin (orange), Ub(t) (chain E), at an r.m.s. deviation of 1. (c) Detailed stereoview of the linkage between the C-terminal Gly76 of ubiquitin and AMP. The corresponding simulated-annealing Fo − Fc map is contoured at an r.m.s. deviation of 3 and is coloured in red. (d) Close-up view of the thioester linkage between the C-terminal Gly76 of Ub(t) and the catalytic Cys600 of Uba1 shown in stereo. The simulated-annealing Fo − Fc map (red mesh) is contoured at an r.m.s. deviation of 2 to reveal some density for the highly mobile residues 73–75 of Ub(t). Difference density in the immediate vicinity of Cys600, which represents the carboxy moiety of Gly76, is clearly visible at an r.m.s. deviation of 3 (cyan mesh). |
![[Figure 2]](be5254fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
