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Plos Biology : Architecture and Selectivity in Aquaporins 2.5 ; Å X-ray Structure of Aquaporin Z, Volume 1

By Simon, Sanford

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Book Id: WPLBN0003921931
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos Biology : Architecture and Selectivity in Aquaporins 2.5 ; Å X-ray Structure of Aquaporin Z, Volume 1  
Author: Simon, Sanford
Volume: Volume 1
Language: English
Subject: Journals, Science, Biology
Collections: Periodicals: Journal and Magazine Collection (Contemporary), PLoS Biology
Historic
Publication Date:
Publisher: Plos

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Simon, S. (n.d.). Plos Biology : Architecture and Selectivity in Aquaporins 2.5 ; Å X-ray Structure of Aquaporin Z, Volume 1. Retrieved from http://netlibrary.net/


Description
Description : Aquaporins are a family of water and small molecule channels found in organisms ranging from bacteria to animals. One of these channels, the E. coli protein aquaporin Z (AqpZ), has been shown to selectively conduct only water at high rates. We have expressed, purified, crystallized, and solved the X-ray structure of AqpZ. The 2.5 A° resolution structure of AqpZ suggests aquaporin selectivity results both from a steric mechanism due to pore size and from specific amino acid substitutions that regulate the preference for a hydrophobic or hydrophilic substrate. This structure provides direct evidence on the molecular mechanisms of specificity between water and glycerol in this family of channels from a single species. It is to our knowledge the first atomic resolution structure of a recombinant aquaporin and so provides a platform for combined genetic, mutational, functional, and structural determinations of the mechanisms of aquaporins and, more generally, the assembly of multimeric membrane proteins.

 

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