|
Figure 2.
Superimposition of haem --HO (green; Sugishima et al.,
2003[triangle]), CN^[minus sign] --haem --HO (yellow, pH 6.8)
and CN^[minus sign] --haem --HO (blue, pH 9.7). Except for the
proximal histidine, only the C^[alpha] traces are shown for
clarity. The crystal structures of CN^[minus sign] --haem --HO
at pH 6.8 and pH 9.7 were superimposed on the structure of haem
--HO so as to minimize the r.m.s. deviations of C^[alpha] atoms.
Following the distal helix is the G-helix, which contains the
basic residues (Lys179 and Arg183) involved in the salt bridges
to haem propionates. Acta Crystallogr Sect F Struct Biol Cryst
Commun. 2007 June 1; 63(Pt 6): 471–474. Published online 2007
May 31. doi: 10.1107/S174430910702475X. Copyright [copyright]
International Union of Crystallography 2007
|
