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Figure 5.
Figure 5. (a) Conformational state surrounding residue 8 in
different mutants and native BmK M1. Residues around position 8
including 8-12 and 63-64 are space-filled and coloured according
to their chemical nature and locations (carbon atoms of residues
8-11 and residue 64 are green and cyan, respectively; nitrogen
and oxygen atoms of these residues are in blue and red,
respectively; two cysteine residues 12 and 63 are yellow).
Broken lines with different colours highlight the surface of
residue 8 (positive, blue; negative, red; neutral, green). (b)
Distinct structures of the five-residue reverse turn (RT) in
association with the C-tail (CT) of the mutants containing trans
peptide bond 9-10 (K8D and K8D/P9S) and cis peptide bond 9-10
(K8Q, K8A and K8G). In the trans-containing form, the peptide
group NH10 is situated inside the turn and residue 8 must be
Asp, which interact with each other via hydrogen bond N10...Od1
8. There is no contact between the NH10 group and the C-terminal
residue, referred to as transRT-freeCT. In cis-containing form
group NH10 points out of the reverse turn and interacts with the
C-terminal residue via hydrogen bond N10...O64, referred to as
cisRT-bondCT. The side-chain of H10 is not shown.
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