 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](ft5125fig2mag.jpg)
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Figure 2
Locations of substitutions and displacements of Cα positions in HN6V (PDB entry 8euo) relative to wild-type HNL from H. brasiliensis. Both figures show the catalytic triad (Ser80, His235 and Asp207) in orange sticks with the Oγ atom of Ser80 in red at the center of the figure. The pink spheres show the Cα atoms of the seven substitutions (Thr11Gly, Glu79His, Cys81Leu, His103Val, Asn104Ala, Gly176Ser and Lys236Met). (a) Ribbon diagram of the X-ray structure of HNL6V (PDB entry 8euo) showing the catalytic domain (α/β-hydrolase fold) in green and the lid domain in blue (residues 115–178). Substitution Gly176Ser is in the lid domain, while the other six are in the catalytic domain. (b) Displacement of Cα positions in HNL6V compared with HbHNL (PDB entry 3c6x). The larger diameter and warmer colors in the cartoon representation indicate larger Cα displacements between structures. The large displacements at the N- and C-termini and the smaller surface-residue displacements are likely to be due to differences in crystallization contacts and unrelated to the substitutions. Among the seven substitutions, only His103Val and Asn104Ala exhibit significant displacement, along with the neighboring residue Ser105. The remaining five substitutions maintain their Cα positions but induce conformational changes in adjacent residues (labeled in turquoise). |
![[Figure 2]](ft5125fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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