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Figure 2.
Figure 2. Structural Comparison of the NBDs of BstUvrA and
Other ABC ATPases
The conserved ATPase motifs are colored
as follows: Walker A/P loop, green; Walker B and D loop, orange;
ABC signature motif, blue; Q loop, magenta; and H loop/switch,
cyan.
(A) Arrangement of the NBDs in E. coli MalK,
Pyrococcus furiosus RLI, and BstUvrA. Key residues important for
nucleotide binding and interactions across the dimer interface
are shown. The transmembrane portion of MalK is depicted in
transparent yellow.
(B) NBDs of UvrA were superimposed with
the NBDs of the maltose transporter MalK (ADP-bound, PDB code
2AWO; ATP-bound, PDB code 1Q12), and Rad50 (ATP-bound, PDB code
1F2U) using their respective ATP-binding domains. All the motifs
are from the same NBD except for the ABC signature motif and the
D loop, which are part of the opposing NBD. The bound ADP is
from the proximal site of UvrA protomer A and is represented as
ball and stick.
(C) Histogram showing the distance between
the C[α] atoms of the conserved Lys residue in the Walker A
motif and Ser residue in the ABC signature motif in the
structures of ABC ATPases solved in the dimeric state (PDB codes
2R6F, 2AWO, 1Q1B, 1Q1E, 2AWN, 1YQT, 1L7V, 2ONK, 1Q12, 1F2U,
1XEF, 1XEX).
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