Unknown

Dataset Information

0

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

altmetric image

Publications

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]

Similar Datasets

| S-EPMC2533189 | biostudies-literature
| S-EPMC4066176 | biostudies-literature
| S-EPMC5813003 | biostudies-literature
| S-EPMC2951199 | biostudies-literature
| S-EPMC2234115 | biostudies-literature
| S-EPMC2885549 | biostudies-literature
| S-EPMC7576499 | biostudies-literature
| S-EPMC2951435 | biostudies-literature
2022-06-28 | GSE206791 | GEO
| S-EPMC4035913 | biostudies-literature