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![[Figure 2]](lp5026fig2mag.jpg)
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Figure 2
Crystallographic structure determination of the ZMPSTE24–phosphoramidon complex. (a) Ribbon diagram of the ZMPSTE24 monomer highlighting the position of the zinc center (gold sphere) and the canonical gluzincin HExxH…E motif (gray sticks). ZMPSTE24 residues His335, His339 and Glu415 are zinc ligands, while Glu336 acts as the catalytic base. Black lines indicate the approximate membrane boundaries. The dashed box indicates the cutaway view used in (b) and (c). (b) The twofold NCS-averaged 2mFo − Fc maps (blue mesh contoured at 1.5σ) and positive mFo − Fc difference map peaks (green mesh contoured at 4.5σ) reveal a molecular envelope consistent with the location of phosphoramidon near the zinc center and the HExxH…E motif. The arrow indicates the putative position of the rhamnose ring of phosphoramidon. (c) The final modeled and refined phosphoramidon molecule (shown in ball-and-stick representation) with overlapping, refined 2mFo − Fc maps (blue mesh contoured at 1.5σ) coordinating the zinc center of ZMPSTE24. The phosphorus atom of the phosphoramidon molecule is colored orange. The phophoramidon specificity pocket-binding moieties tryptophan (P2′) and leucine (P1′) are explicitly labeled for clarity. |
![[Figure 2]](lp5026fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
