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Figure 3.
Figure 3. Interactions within the helical scaffold domain
and within the dimer interface. (a) The swiveling of the
C-terminal domain of helix 1 of hsd is propagated via van der
Waals interactions between Ile610 and Trp724. The conserved salt
bridge between Arg614 and Asp721 is broken in the new structure
presented here. Arrows indicate the direction of movement of
secondary structure elements. Right panel: a magnified view of
the B. subtilis SecA structure (pdb code 1M6N, gray)
superimposed on subunit a of the new SecA dimer (orange). (b)
Asn588 of helix 1 in the helical scaffold domain is located at
the dimer interface. Replacement by cysteine can be used to form
disulfide-linked monomers.
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