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Figure 3
(a) Superimposition of the [Mtb{\rm EccC_5^{DUF}}] (green) and SrsEssCD3 (PDB entry 6vt1, dark blue) crystal structures showing details of their degenerated ATP-binding sites. Residues occupying key positions for nucleotide/magnesium interaction and hydrolysis are labelled and represented as sticks. The Walker A, Walker B and Sensor 1 motifs of [Mtb{\rm EccC_5^{DUF}}] are coloured following the same colour code as in Fig. 2[link]. (b) Superimposition of [Mtb{\rm EccC_5^{DUF}}] DSF profiles in the absence (control) and presence of ADP–AlF3 (4 mM) and Mg2+ (5 mM). The failure of ADP–AlF3/Mg2+ to stabilize the domain structure against thermal denaturation was consistent with a lack of nucleotide binding. (c) ITC titration of ATP (1.3 mM) into [{\rm EccC_5^{DUF}}] (60 µM) and buffer C (black and blue data, respectively). The upper and lower panels show raw thermograms and normalized heat effect per mole of ATP injected versus ATP:[{\rm EccC_5^{DUF}}] molar ratio, respectively.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 80| Part 6| June 2024| Pages 397-409
https://doi.org/10.1107/S2059798324004248
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