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Figure 6
(a) Overview of the 1.7 Å resolution crystal structure of ctMex67UBA. Like other UBA domains of Mex67/NXF1 from H. sapiens and S. cerevisiae, the domain was based on three principal α-helices together with the extreme C-terminal region that formed contacts with the first α-helix (α1). (b) Schematic illustration of the secondary-structural elements in the UBA domain. (c) Detailed view of the dimethylarsenic group conjugated to Cys623 of ctMex67. An anomalous difference Fourier contoured at 6σ (represented in blue) showed clear density around the As atom. (d) Surface representation of the FG nucleoporin binding site present in the UBA domains of ctMex67 (left) and hsNXF1 (right). The UBA domain from ctMex67 clearly has the same binding pocket as present in hsNXF1, although the dimethylarsenic group described in (c) was found to be bound there. (e) Three representative views of the final 2FoFc map for the ctMex67UBA structure contoured at the 1σ level.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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