2h2s

Crystal Structure of E148A mutant of CLC-ec1 in SeCN-Crystal Structure of E148A mutant of CLC-ec1 in SeCN-

Structural highlights 2h2s is a 6 chain structure with sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 1ots, 2h2p Gene: clcA, eriC (Escherichia coli) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class of proteins that catalyze transmembrane exchange of Cl- and H+ necessary for pH regulation of numerous physiological processes. Despite a profusion of high-resolution structures, the molecular mechanism of exchange remains unknown. Here, we rigorously demonstrate strict exchange stoichiometry of 2 Cl-/1 H+. In addition to Cl- and Br-, two non-halide ions, NO3- and SCN-, are shown to be transported by CLC-ec1, but with reduced H+ counter-transport. The loss of proton coupling to these anions is accompanied by an absence of bound anions in the central and external Cl- binding sites in the protein's anion selectivity region, as revealed by crystallographic comparison of Br- and SeCN- bound to this region. Uncoupling of a CLC Cl-/H+ exchange transporter by polyatomic anions.,Nguitragool W, Miller C J Mol Biol. 2006 Sep 29;362(4):682-90. Epub 2006 Aug 14. PMID:16905147 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monoclonal Antibody

spinqualitylabelsall models 2h2s, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image