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Figure 3.
Figure 3. TEM-1 -BLIP interface. a, BLIP (blue) binds
competitively to TEM-1 (orange). BLIP has an overall  -saddle
fold consisting of two tandem repeats. The large concave
eight-stranded -sheet
of BLIP wraps around the TEM-1 loop-helix region (green). Asp 49
and Phe 142 on the protruding -hairpin
turns of BLIP insert into the TEM-1 active site cavity and
structurally mimic the carboxylate and benzyl side chain of a
penicillin substrate. To illustrate the competitive mode of
inhibition, the penicilloyl moiety (thin stick rendering) of the
TEM-1 -penicillin G acyl-enzyme intermediate^13 is superimposed
on the active site region of the complex. b, Interface between
BLIP (blue) and the TEM-1 loop-helix region (residues 99 -114
shown in stick rendering with green carbons). For clarity, the
side chains of Asp 101, Thr 109 and His 112 on TEM-1 were
omitted.
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