Crystal structure of guanosine 5′-monophosphate synthetase from the thermophilic bacterium Thermus thermophilus HB8

Nemoto, N.; Baba, S.; Kawai, G.; Sampei, G.

doi:10.1107/S2053230X2400877X

Figure 3
Conformational fluctuations of the TtGuaA model deduced from analysis of the MD simulations. Atomic fluctuations are represented for each amino-acid residue as the scale of the B factor. (a) Fluctuations of the whole structure of subunits A (blue) and B (red). Two disordered regions (D1 and D2) are indicated by bidirectional arrows. (b) The fluctuations of subunit A when the GATase domain (1–185) of subunit A (gray), the ATPPase domain (192–389) of subunit A (blue) and the dimerization domain (396–503) of subunit A (orange) were fixed. (c) The fluctuations of subunit A when the GATase domain of subunit B (gray), the ATPPase domain of subunit B (blue) and the dimerization domain of subunit B (orange) were fixed. (d) The fluctuations of subunit B when the GATase domain of subunit A (gray), the ATPPase domain of subunit A (blue) and the dimerization domain of subunit A (orange) were fixed. (e) The fluctuations of subunit B when the GATase domain of subunit B (gray), the ATPPase domain of subunit B (blue) and the dimerization domain of subunit B (orange) were fixed. (f) The fluctuations of the ligands and Mg²⁺ ion when subunits A and B (All) or three domains (GATase domain, GAT; ATPPase domain, CAT; dimerization domain, DD) of each subunit were fixed. The bars of the fluctuations are colored as follows: XMP in subunit A, blue; ATP in subunit A, orange; Mg²⁺ in subunit A, gray; XMP in subunit B, yellow; ATP in subunit B, cyan; Mg²⁺ in subunit B, green.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 80| Part 10| October 2024| Pages 278-285

https://doi.org/10.1107/S2053230X2400877X

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