1RC2

2.5 Angstrom Resolution X-ray Structure of Aquaporin Z

Summary for 1RC2

• Entry DOI: 10.2210/pdb1rc2/pdb
• Descriptor: Aquaporin Z, 2-O-octyl-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: aquaporin, membrane protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 48604.80

Authors

Savage, D.F.,Egea, P.F.,Robles, Y.C.,O'Connell III, J.D.,Stroud, R.M. (deposition date: 2003-11-03, release date: 2003-11-25, Last modification date: 2023-08-23)

Primary citation

Savage, D.F.,Egea, P.F.,Robles-Colmenares, Y.,O'Connell III, J.D.,Stroud, R.M.
Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z
Plos Biol., 1:334-340, 2003

PubMed 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.

PubMed: 14691544
DOI: 10.1371/journal.pbio.0000072

Experimental method

X-RAY DIFFRACTION (2.5 Å)