2o9f
From Proteopedia
(New page: 200px<br /><applet load="2o9f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o9f, resolution 2.550Å" /> '''Crystal Structure o...) |
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| - | [[Image:2o9f.jpg|left|200px]]<br /><applet load="2o9f" size=" | + | [[Image:2o9f.jpg|left|200px]]<br /><applet load="2o9f" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2o9f, resolution 2.550Å" /> | caption="2o9f, resolution 2.550Å" /> | ||
'''Crystal Structure of AqpZ mutant L170C'''<br /> | '''Crystal Structure of AqpZ mutant L170C'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2O9F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 2O9F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O9F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: integral membrane protein]] | [[Category: integral membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:31:46 2008'' |
Revision as of 13:31, 23 January 2008
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Crystal Structure of AqpZ mutant L170C
Overview
The aquaporin family of channels was defined based on the inhibition of, water transport by mercurial compounds. Despite the important role of, mercurials, little is known about the structural changes involved upon, mercury binding leading to channel inhibition. To elucidate the mechanism, we designed a mutant, T183C, of aquaporin Z (AqpZ) patterned after the, known mercury-sensitive site of aquaporin 1 (AQP1) and determined the, X-ray crystal structures of the unbound and mercury blocked states., Superposition of the two structures shows no conformational rearrangement, upon mercury binding. In the blocked structure, there are two mercury, sites, one bound to Cys183 and occluding the pore, and a second, also, bound to the same cysteine but found buried in an interstitial cavity. To, test the mechanism of blockade we designed a different mutant, L170C, to, produce a more effective mercury block at the pore site. In a, dose-response inhibition study, this mutant was 20 times more sensitive to, mercury than wild-type AqpZ and four times more sensitive than T183C. The, X-ray structure of L170C shows four mercury atoms at, or near, the pore, site defined in the T183C structure and no structural change upon mercury, binding. Thus, we elucidate a steric inhibition mechanism for this, important class of channels by mercury.
About this Structure
2O9F is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural basis of aquaporin inhibition by mercury., Savage DF, Stroud RM, J Mol Biol. 2007 May 4;368(3):607-17. Epub 2007 Mar 2. PMID:17376483
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