Volume 3, Issue 8, Pages 781-790 (August 1995) Structural evidence for the evolutionary divergence of mycoplasma from Gram-positive bacteria: the histidine-containing phosphocarrier protein  Ursula Pieper, Geeta Kapadia, Peng-Peng Zhu, Alan Peterkofsky, Osnat Herzberg  Structure  Volume 3, Issue 8, Pages 781-790 (August 1995) DOI: 10.1016/S0969-2126(01)00213-1

Figure 1 Stereoview of the Fourier electron-density map associated with (a) residues 10, 14–17 and (b) 44–47 in HPr from M. capricolum. The coefficients 2Fo–Fc and calculated phases are used. The maps are contoured at the 1σ level. No electron density is associated with the side chain of Arg17 beyond Cδ. (Figure drawn using TURBO-FRODO [37].) Structure 1995 3, 781-790DOI: (10.1016/S0969-2126(01)00213-1)

Figure 1 Stereoview of the Fourier electron-density map associated with (a) residues 10, 14–17 and (b) 44–47 in HPr from M. capricolum. The coefficients 2Fo–Fc and calculated phases are used. The maps are contoured at the 1σ level. No electron density is associated with the side chain of Arg17 beyond Cδ. (Figure drawn using TURBO-FRODO [37].) Structure 1995 3, 781-790DOI: (10.1016/S0969-2126(01)00213-1)

Figure 2 The overall fold of HPr from M. capricolum. The active-site residue, His15, and Ser46 with its associated sulfate ion are shown in ball-and-stick representation. (Figure drawn with MOLSCRIPT [41].) Structure 1995 3, 781-790DOI: (10.1016/S0969-2126(01)00213-1)

Figure 3 Superposition of the crystal structures of HPr from M. capricolum (red, MC), B. subtilis (high-salt crystal, dark blue; low-salt crystal, magenta), E. coli (yellow) and S. faecalis (green). Virtual bonds between Cα atoms are drawn. (Figure drawn with SETOR [42].) Structure 1995 3, 781-790DOI: (10.1016/S0969-2126(01)00213-1)

Figure 4 Stereo representation of the active-site region of HPr from M. capricolum including residues 10–18 [44]. Only part of the side chain is shown because it is disordered beyond the Cδ atom. (Figure drawn with PLUTO [44].) Structure 1995 3, 781-790DOI: (10.1016/S0969-2126(01)00213-1)

Figure 5 Superposition of the active-site regions of the crystal structures of HPr from M. capricolum (red), B. subtilis (high-salt crystal, blue; low-salt crystal, purple), E. coli (yellow) and S. faecalis (green). Virtual bonds between Cα atoms are traced. The complete side chains of His15, Arg17 (except for M. capricolum), Asp10 (only for M. capricolum) and the sulfate ions found in two structures are also shown. Structure 1995 3, 781-790DOI: (10.1016/S0969-2126(01)00213-1)

Figure 6 Stereoview of the environment of the sulfate ion. This includes residues 45–49 and Lys3 and Lys11 of symmetry-related molecules. Structure 1995 3, 781-790DOI: (10.1016/S0969-2126(01)00213-1)

Figure 7 Stereoview of the superposition of residues 53–55 and 37 of HPr from M. capricolum (red), B. subtilis (high-salt crystal, purple), E. coli (yellow) and S. faecalis (green), including a sulfate ion present in the E. coli structure. The E. coli structure adopts a different main-chain conformation in this region from that seen in structures from Gram-positive bacteria and mycoplasma. Structure 1995 3, 781-790DOI: (10.1016/S0969-2126(01)00213-1)

Figure 8 Stereoview of the superposition of the N and C termini of HPr from M. capricolum (red), B. subtilis (high-salt crystal, purple), E. coli (yellow) and S. faecalis (green). Main-chain atoms of residues 6–18 and from 78 to their respective C termini are shown. The side chains of His15 and Glu85 of the E. coli (EC) HPr are also drawn. Structure 1995 3, 781-790DOI: (10.1016/S0969-2126(01)00213-1)

Figure 9 Stereoview of the environment of the type II′ reverse turn centered on residues 38 and 39. This includes residues 36-41 of one molecule and residues 27–31 of a symmetry-related molecule (indicated by #). Structure 1995 3, 781-790DOI: (10.1016/S0969-2126(01)00213-1)