1rc2
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= AQPZ, BNIP, B0875, C1009, SF0832, S0873 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= AQPZ, BNIP, B0875, C1009, SF0832, S0873 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rc2 OCA], [http://www.ebi.ac.uk/pdbsum/1rc2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rc2 RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Savage, D F.]] | [[Category: Savage, D F.]] | ||
[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
| - | [[Category: BGL]] | ||
[[Category: aquaporin]] | [[Category: aquaporin]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:26:04 2008'' |
Revision as of 20:26, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | AQPZ, BNIP, B0875, C1009, SF0832, S0873 (Escherichia coli) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 23:26:04 2008
