Journal:JMB:2
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | Old rePON1 at pH 4.5<scene name= | + | Old rePON1 at pH 4.5<scene name=Journal:JMB:2/New_no_hq/4'>TextToBeDisplayed</scene> |
New rePON1 at pH 6.4<scene name='Journal:JMB:2/First/2'>TextToBeDisplayed</scene> | New rePON1 at pH 6.4<scene name='Journal:JMB:2/First/2'>TextToBeDisplayed</scene> | ||
Revision as of 12:13, 7 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
Old rePON1 at pH 4.5 New rePON1 at pH 6.4
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).
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