Conformational changes induced upon ligand-binding in AckAs. (A) Structural comparison of A-subunit of Form-I StAckA (apo, pink) with open (yellow) and closed (cyan) subunits of MtAckA (PDB:1TUY). A large movement in domain-I (moving domain) relative to the domain-II (fixed domain) could be observed. Regions connecting the two domains are represented by the putative hinge residues (Ala152 and Thr385). N- and C-termini as well as secondary structures corresponding to the core helices are labeled. (B) Influence of ligand binding on the intrinsic fluorescence (excitation: 280 nm, emission: 300–400 nm) of StAckA.
Chittori et al. BMC Structural Biology 2012 12:24 doi:10.1186/1472-6807-12-24