 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](ft5122fig3mag.jpg)
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Figure 3
(a) The dimeric substructure of His-GsePNPase. The two subunits are independently coloured and the regions of each corresponding to the N-terminal tag are coloured yellow. The position of the N-terminal tag indicates the approximate position of the active sites in each dimer, which sit at the interface between the subunits. (b) A structural overlay of EcPNPase (PDB entry 1pk7, white) and His-GsePNPase (subunit a in blue and subunit b in green) highlighting the conservation of the active-site residues. Adenine and phosphate from the EcPNPase structure are coloured yellow. Putative hydrogen-bonding interactions between these molecules and the EcPNPase residues are shown as dashed lines. (c) Overlay of the Tyr5 residue from the rTEV site (yellow) and the adenine base from PDB entry 1k9s (white). (d) The segmenting H7 in the two different positions found in EcPNPase (closed, dark grey; open, white, from PDB entry 1k9s chains A and D) and the position of this region in His-GsePNPase (blue; the N-terminal tag is shown in yellow). |
![[Figure 3]](ft5122fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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