Structural and functional analysis of the d-alanyl carrier protein ligase DltA from Staphylococcus aureus Mu50

Lee, I.-G.; Song, C.; Yang, S.; Jeon, H.; Park, J.; Yoon, H.-J.; Im, H.; Kang, S.-M.; Eun, H.-J.; Lee, B.-J.

doi:10.1107/S2059798322000547

Figure 1
Overall structure of SaDltA. (a) Ribbon diagram and surface representation of two perpendicular views of SaDltA (the N-terminal lobes and C-terminal lobes are colored orange and blue, respectively). The ATP molecule bound in the active site is shown using a stick representation and is colored by atom type. (b) Sequence conservation of SaDltA (see also Fig. 2

) mapped onto the surface of the structure and colored from low to high conservation using a red to green gradient. (c) Left: close-up view showing the ATP- and Mg²⁺-bound active site of SaDltA. The 2F_o − F_c electron-density map (gray mesh) contoured at 1.0σ is shown around an all-atom representation of the P-loop. Center: close-up view showing the ATP- and Mg²⁺-bound active site of B. cereus DltA (PDB entry 3fcc). Right: close-up view showing the D-alanine-adenylate-bound active site of B. cereus DltA (PDB entry 3dhv). (d) B-factor distribution mapped onto the surface of SaDltA chains A and B (left) or chains C and D (right). The B-factor distribution is colored from low (20 Å²) to high (90 Å²) using a blue to red gradient. (e) Close-up view showing the interaction between the P-loop and residues residing in the hinge region of the Ppant blocking loop. Chain A of SaDltA is colored orange (N-lobe) and blue (C-lobe) and chain C of SaDltA is colored gray.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 78| Part 4| April 2022| Pages 424-434

https://doi.org/10.1107/S2059798322000547

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