PMID:14691544
| Citation |
Savage, DF, Egea, PF, Robles-Colmenares, Y, O'Connell, JD 3rd and Stroud, RM (2003) Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z. PLoS Biol. 1:E72 |
|---|---|
| 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 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. |
| Links |
PubMed PMC300682 Online version:10.1371/journal.pbio.0000072 |
| Keywords |
Amino Acid Sequence; Aquaporins/chemistry; Aquaporins/isolation & purification; Carbon/chemistry; Cell Membrane/metabolism; Crystallography, X-Ray; Detergents/pharmacology; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/isolation & purification; Glycerol/chemistry; Hydrogen/chemistry; Membrane Proteins/chemistry; Membrane Proteins/isolation & purification; Models, Molecular; Molecular Conformation; Molecular Sequence Data; Oxygen/chemistry; Protein Binding; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins/chemistry; Sequence Homology, Amino Acid; Water/chemistry |
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