 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](ih5007fig2mag.jpg)
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Figure 2
(a) Superposition of apo and atorvastatin-bound hHMGR cryo-EM structures. The atorvastatin-bound structure is shown in cartoon representation, coloured based on residue Cα deviations calculated against the apo structure on a linear blue–white–red scale with increasing magnitude. The maximum deviation is observed for the N-terminus of the N-domain. Atorvastatin bound in the four different active sites is also shown in ball-and-stick representation in grey. (b) Comparison of the crystal and cryo-EM structures of atorvastatin-bound hHMGR. The atorvastatin-bound cryo-EM structure (PDB entry 8pkn) is coloured based on residue Cα deviations calculated against the atorvastatin-bound crystal structure (PDB entry 1hwk) in blue–white–red with increasing magnitude. Apart from the loop regions being flexible, the N-domain, which functionally connects the catalytic portion of the enzyme to the membrane domain, is found to have relatively high deviations. The regions coloured in grey are those without equivalent residues in the crystal structure for comparison. |
![[Figure 2]](ih5007fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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