Journal:JMB:2
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | Figure 2. Structural details of the 2HQ/rePON1 complex at pH 6.5;; (A)<scene name='Journal:JMB:2/2a/ | + | Figure 2. Structural details of the 2HQ/rePON1 complex at pH 6.5;; (A)<scene name='Journal:JMB:2/2a/2'>TextToBeDisplayed</scene> 2HQ and the |
structured active-site loop in the rePON1-2HQ complex structure. The Fo-Fc omit map is | structured active-site loop in the rePON1-2HQ complex structure. The Fo-Fc omit map is | ||
contouered at B) Overlay of the phosphate ion in the apo rePON1 at pH 6.5 and of 2HQ | contouered at B) Overlay of the phosphate ion in the apo rePON1 at pH 6.5 and of 2HQ | ||
Revision as of 16:09, 6 March 2012
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Title Of The Paper
Authors[1]
Molecular Tour
Figure 2. Structural details of the 2HQ/rePON1 complex at pH 6.5;; (A) 2HQ and the
structured active-site loop in the rePON1-2HQ complex structure. The Fo-Fc omit map is
contouered at B) Overlay of the phosphate ion in the apo rePON1 at pH 6.5 and of 2HQ
in the rePON1-2HQ complex. (C) The first segment of the active-site loop, and residues Y71
and I74 in particular, comprises part of PON1's active-site wall. (D) Interactions of 2HQ with
active-site residues (interactions with the catalytic Ca2+ are highlighted in red).
Figure 3. 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.
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