 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 6]](jt5072fig6mag.jpg)
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Figure 6
Clustered, correlated conformations localize to functionally linked and/or ligandable sites. Two sub-clusters of alternate conformations are identified, with one around the BB site (Wiesmann et al., 2004  ) and the other not previously reported in the allosteric network. Since these two sub-clusters are bridged by the functionally linked Phe225 (Torgeson et al., 2022), they cohere as a single coupled cluster. (a, b) Our new high-resolution apo WT structure (chain A, cyan; chain B, maroon) and electron density (2Fo − Fc map in blue mesh, 1σ). We observe two adjacent sub-clusters with correlated alternate conformations. One involves the BB pathway (Phe191) and the other has not previously been reported as allosteric. (c) One of the two sub-clusters is also adjacent to recently reported small-molecule fragments that bind in the adjacent BB allosteric site, from the only structure series in the same crystal form as our structure (PDB entry 8g6a chain A, olive; PDB entry 8g67 chain A, orange; Greisman, Willmore et al., 2023). (d) The two sub-clusters are also adjacent to several residues shown to influence activity upon mutation, including Phe225 which bridges the two sub-clusters (Torgeson et al., 2022). Here, we show an overlay of the F225Y–R199N double-mutant structure (pink, PDB entry 7mn9) with our WT structure. Additional remodeled conformations that were originally missing (see Fig. 5) are colored brown. |
![[Figure 6]](jt5072fig6.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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