Journal:JMB:2
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | <scene name='Journal:JMB:2/Scene_1/3'> | + | Previously PON1 was <scene name='Journal:JMB:2/Scene_1/3'>solved at 4.5 pH</scene>. The authors sought a physiologically active pH and<scene name='Journal:JMB:2/Scene_2/1'>solved PON1 at 6.5 pH overlain with 4.5</scene>. Note <scene name='Journal:JMB:2/Scene_3/1'>residues 346-348 in the two structures</scene>. Especially, observe the <scene name='Journal:JMB:2/Scene_4/1'>movement of residue 71</scene>. The authors also solved PON1 at 6.5 pH in <scene name='Journal:JMB:2/Scence_5/3'>complex with 2HQ (a lactone approximate)</scene>. Here, the authors for the first time observe ordered<scene name='Journal:JMB:2/Scene_6/1'>active site loop density</scene>. |
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Revision as of 21:34, 19 March 2012
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Catalytic versatility and backups in enzyme active sites: The case of serum paraoxanase 1
Moshe Ben-David, Mikael Elias, Jean-Jacques Filippi, Elisabet Dunach, Israel Silman, Joel Sussman and Dan Tawfik, PhD [1]
Molecular Tour
Previously PON1 was . The authors sought a physiologically active pH and. Note . Especially, observe the . The authors also solved PON1 at 6.5 pH in . Here, the authors for the first time observe ordered. or without labels
Figure 2. Structural details of the 2HQ/rePON1 complex at pH 6.5; 2HQ and the structured active-site loop in the rePON1-2HQ complex structure. Overlay of the phosphate ion in the apo rePON1 at pH 6.5 and of 2HQ in the rePON1-2HQ complex. The first segment of the active-site loop, and residues Y71 and I74 in particular, comprises part of PON1's active-site wall. Interactions of 2HQ with active-site residues (interactions with the catalytic Ca2+ are highlighted in red).
. Changes in the rePON1 binding site upon binding of 2HQ. Superimposition of the rePON1-2HQ complex (cyan; the closed conformation) with the apo rePON1 structures at pH 4.5 (orange) and pH 6.5 (blue) (the open conformations). The pH 4.5 conformation prevents closure of the active-site loop due to clashes of F347 and H348 with the loop residues (e.g. F77 and I74). Also illustrated is the movement of Y71 (dashed arrow) upon binding of 2HQ, and its interaction with D183 in the 2HQ complex structure.
- ↑ Ben-David M, Elias M, Filippi JJ, Dunach E, Silman I, Sussman JL, Tawfik DS. Catalytic Versatility and Backups in Enzyme Active Sites: The Case of Serum Paraoxonase 1. J Mol Biol. 2012 Mar 1. PMID:22387469 doi:10.1016/j.jmb.2012.02.042
