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Figure 5
The ubiquitin-adenylate in comparison to other Ub(a) structures and the MoaD-adenylate. In the left panels an overview of the UBL (yellow) is shown bound to the respective activating enzymes colour-coded as described in Fig. 4[link] but rendered with a higher transparency. The right panels show a detailed view of the respective adenylation active site including critical residues. Hydrogen bonds are indicated as dashed lines. Structures of (a) Uba1–Ub from S. cerevisiae in the absence of ATP (PDB entry 3cmm), (b) Uba1–Ub–ATP from S. pombe (PDB entry 4ii3), (c) Uba1–Ub(a)–Ub(t) from S. cerevisiae including the ubiquitin-adenylate (PDB entry 4nnj) and (d) E. coli MoeB–MoaD including the MoaD-adenylate (PDB entry 1jwb). MoeB is coloured green, while the second MoeB monomer in the heterotetrameric MoaB–MoaD structure and the critical Arg14 are coloured purple.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 70| Part 5| May 2014| Pages 1311-1320
https://doi.org/10.1107/S1399004714002910
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