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- Title
Architecture and Selectivity in Aquaporins: 2.5 Å X-Ray Structure of Aquaporin Z.
- Authors
Savage, David F; Egea, Pascal F; Robles-Colmenares, Yaneth; III, Joseph D. O'Connell; Stroud, Robert M
- Abstract
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 Å 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. The 2.5 Å resolution structure of the E. coli water- specific aquaporin AqpZ provides direct evidence for the molecular mechanisms of specificity for water, as opposed to glycerol, in this family of channels.
- Subjects
AQUAPORINS; ESCHERICHIA coli; MEMBRANE proteins; SMALL molecules; X-rays; ATOMIC structure
- Publication
PLoS Biology, 2003, Vol 1, Issue 12, p1
- ISSN
1544-9173
- Publication type
Article
- DOI
10.1371/journal.pbio.0000072