Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z.

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 recombinan

SUBMITTER: Savage DF 

PROVIDER: S-EPMC300682 | biostudies-literature | 2003 Dec

REPOSITORIES: biostudies-literature