1rc2
From Proteopedia
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'''2.5 Angstrom Resolution X-ray Structure of Aquaporin Z''' | '''2.5 Angstrom Resolution X-ray Structure of Aquaporin Z''' | ||
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[[Category: Savage, D F.]] | [[Category: Savage, D F.]] | ||
[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
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Revision as of 04:19, 3 May 2008
2.5 Angstrom Resolution X-ray Structure of Aquaporin Z
Overview
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.
About this Structure
1RC2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z., Savage DF, Egea PF, Robles-Colmenares Y, O'Connell JD 3rd, Stroud RM, PLoS Biol. 2003 Dec;1(3):E72. Epub 2003 Dec 22. PMID:14691544 Page seeded by OCA on Sat May 3 07:19:13 2008
