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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 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.

SUBMITTER: Savage DF 

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

REPOSITORIES: biostudies-literature

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

Savage David F DF   Egea Pascal F PF   Robles-Colmenares Yaneth Y   O'Connell Joseph D JD   Stroud Robert M RM  

PLoS biology 20031222 3


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 regu  ...[more]

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