Fig. 5: Increased protein stability towards hydrostatic pressure in the MHS. | Nature Ecology & Evolution

Fig. 5: Increased protein stability towards hydrostatic pressure in the MHS.

From: Morphology and genome of a snailfish from the Mariana Trench provide insights into deep-sea adaptation

Fig. 5

a, Model of the evolution of the gene encoding the TMAO-generating enzyme flavin monooxygenase 3. b, A maximum-likelihood tree and alignment of fish hsp90 sequences within five clades. Amino acids unique to the MHS are highlighted in red. c, Three-dimensional views of the hsp90 protein (hadal12091 is shown as an example; others are shown in Supplementary Fig. 36), highlighting MHS-specific amino acid substitutions. The homology model of the overall amino acid sequence is shown to the left; Ser202 atoms (coloured cyan) are shown as spheres. The expansion shows a model of the N-terminal domain, with the ligand-binding pocket coloured orange and shown in surface mode.

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