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Figure 2.
Figure 2. Overall Fold of AAC(6′)-Iy(A) The
crystallographically determined structure of the S. enterica
AAC(6′)-Iy monomer. The coloring conforms to the
amino-terminal residues (β1, α1, α2, green), the central β
strands (β2–4, yellow), the central α helix and β strand
(α3, β5, red), and the carboxy-terminal region (α4, β6,
blue). CoenzymeA and ribostamycin are colored by atom type. This
coloring scheme is used throughout.(B) The S. enterica
AAC(6′)-Iy dimer showing the position of bound CoA and
ribostamycin (stick representation, colored by atom type). The
exchange of the β6 and β6′ strands is noted.(C) The
interaction between two S. enterica AAC(6′)-Iy dimers showing
the N terminally extended peptide, colored by atom type,
interacting with an adjacent dimer.(D) Closeup of the
interaction between the crystallographically observable N
terminally extended peptide and the active site channel. The
dimer is presented in surface representation with each monomer
colored in silver or bronze.
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