 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](ih5007fig1mag.jpg)
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Figure 1
(a) The flexible N-domain. The commonly disordered region, which is part of the N-domain (residues 439–487) of the enzyme, is ordered in the cryo-EM structures and is modelled completely. The built model of the region is shown with side chains in ball-and-stick representation and coloured white. The locspiral-sharpened cryo-EM map is shown at a threshold level of 6 (for ChimeraX; volume zone nearAtoms range of 4.5 Å) in cornflower blue in mesh representation and several residues along the chain are labelled. (b) Atorvastatin density. The cryo-EM map at a threshold level of 3.5 (for ChimeraX; volume zone nearAtoms range of 3 Å) of atorvastatin is coloured in cornflower blue in mesh representation. The atorvastatin model is rendered in ball-and-stick representation (in cornflower blue for cryo-EM and in purple for the crystal structure PDB entry 1hwk). The atorvastatin binding seen in the cryo-EM sample is almost identical to the crystal structure conformation. (c, d) Active-site residues around atorvastatin. All residues in close contact with the inhibitor are shown in ball-and-stick representation. The corresponding residues in the apo enzyme are shown in green (c) and are partially transparent in the atorvastatin-bound structure (the residues belonging to two different monomers are shown in yellow and blue). The residues from the crystal structure (PDB entry 1hwk) are depicted in pink (d). For clarity, the residues are only labelled in (c) and the labelling holds true for (d). No noticeable change can be seen in the conformation of residues due to binding of the inhibitor to the active site. |
![[Figure 1]](ih5007fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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