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Figure 5 | BMC Structural Biology

Figure 5

From: Structural and mechanistic investigations on Salmonella typhimurium acetate kinase (AckA): identification of a putative ligand binding pocket at the dimeric interface

Figure 5

Conformational changes induced upon ligand-binding in AckAs. (A) Structural comparison of A-subunit of Form-I St AckA (apo, pink) with open (yellow) and closed (cyan) subunits of Mt AckA (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 St AckA.

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BMC Structural Biology

ISSN: 1472-6807

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