Fig. 2.

Different properties of residues in the Ba2390 structures plotted as a function of residue number. (a) A plot of the atom contacts between molecules in crystal lattice: red - residues forming close contacts (from 2.0 to 3.5 Å), green - residues forming hydrogen bonds, pale blue – residues bridged by water molecule, grey - residues forming other contacts (from 3.5 to 4.5 Å). The top graph represents contacts in the structure of the apo-form of BA2930, and the bottom in the CoA-bound structure. Contacts and distances were calculated using the CONTACT program from the CCP4 suite. (b) Plot of the RMSD and distance profiles comparing the apo and CoA-bound structures. Blue lines - RMSD values between corresponding residues. Red lines - distances between corresponding Cα atoms. The pale, thin lines represent pairwise chain comparisons between structures. Averaged results using a window of 4 comparisons are plotted with bold lines. (c) Cα distances between superposed A and B chains from one structure. The structure of the apo-form of BA2930 is represented in orange and the CoA-bound structure in green. (d) Percent deviation of the Cα temperature factors from the average value. All calculations were performed with the BioShell package.⁴³ Superposition of two BA2930 subunits yields Cα RMSD values of 0.4 Å for both apo- and CoA-bound forms of BA2930. Superposition of each chain of the apo-form on the corresponding chain of the CoA-bound form yields Cα RMSD values ranging from 0.3 to 0.4 Å. These differences can be attributed to mentioned before putative substrate binding lobe. We also observe a similar degree of flexibility in the crystallized mutants (data not shown).