1rc2
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(New page: 200px<br /><applet load="1rc2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rc2, resolution 2.5Å" /> '''2.5 Angstrom Resoluti...)
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Revision as of 23:19, 20 November 2007
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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 with BGL as ligand. 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
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