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. 2013 Sep 20;69(Pt 10):2061–2071. doi: 10.1107/S0907444913019197

Figure 4.

Figure 4

Stereoview of interactions associated with the α- (ζ-) and β-subunit C-termini in the T (PDB entries 2hhb or 2dn2; cyan), R (PDB entries 1aj9 or 1ljw; red), Hb ζ2β2 s ABCD (yellow) and/or EFGH (gray) structures. (a) The T-state salt-bridge interaction between β1His146 and β1Asp94 is broken in the R structure but is maintained in the liganded Hb ζ2β2 s structure. (b) The T-state salt-bridge interactions between α1Arg141 and α2Lys120 and α2Asp126 are broken in both the R and the liganded Hb ζ2β2 s structures. (c) Reorientation of the Hb ζ2β2 s ABCD ζ-subunit C-terminus results in hydrogen-bond interactions between ζ1Arg141 and the F-helix residues ζ1Arg92, ζ1Asp94 and ζ1Glu138. The corresponding interactions in the EFGH tetramer are missing owing to disorder of the ζArg141 residue.