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| - | [[Image:2htk.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2htk| PDB=2htk | SCENE= }} | | {{STRUCTURE_2htk| PDB=2htk | SCENE= }} |
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| - | '''Structure of the Escherichia coli ClC chloride channel Y445A mutant and Fab complex'''
| + | ===Structure of the Escherichia coli ClC chloride channel Y445A mutant and Fab complex=== |
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| - | ==Overview==
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| - | The Cl-/H+ exchange-transporter CLC-ec1 mediates stoichiometric transmembrane exchange of two Cl- ions for one proton. A conserved tyrosine residue, Y445, coordinates one of the bound Cl- ions visible in the structure of this protein and is located near the intersection of the Cl- and H+ pathways. Mutants of this tyrosine were scrutinized for effects on the coupled transport of Cl- and H+ determined electrophysiologically and on protein structure determined crystallographically. Despite the strong conservation of Y445 in the CLC family, substitution of F or W at this position preserves wild-type transport behavior. Substitution by A, E, or H, however, produces uncoupled proteins with robust Cl- transport but greatly impaired movement of H+. The obligatory 2 Cl-/1 H+ stoichiometry is thus lost in these mutants. The structures of all the mutants are essentially identical to wild-type, but apparent anion occupancy in the Cl- binding region correlates with functional H+ coupling. In particular, as determined by anomalous diffraction in crystals grown in Br-, an electrophysiologically competent Cl- analogue, the well-coupled transporters show strong Br- electron density at the "inner" and "central" Cl- binding sites. However, in the uncoupled mutants, Br- density is absent at the central site, while still present at the inner site. An additional mutant, Y445L, is intermediate in both functional and structural features. This mutant clearly exchanges H+ for Cl-, but at a reduced H+-to-Cl- ratio; likewise, both the central and inner sites are occupied by Br-, but the central site shows lower Br- density than in wild-type (or in Y445F,W). The correlation between proton coupling and central-site occupancy argues that halide binding to the central transport site somehow facilitates movement of H+, a synergism that is not readily understood in terms of alternating-site antiport schemes. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16949616}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16949616 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16949616}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: H+/cl- antiporter]] | | [[Category: H+/cl- antiporter]] |
| | [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:41:40 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:11:15 2008'' |
Revision as of 23:11, 27 July 2008
Template:STRUCTURE 2htk
Structure of the Escherichia coli ClC chloride channel Y445A mutant and Fab complex
Template:ABSTRACT PUBMED 16949616
About this Structure
2HTK is a Single protein structure of sequence from Escherichia coli and Mus musculus. Full crystallographic information is available from OCA.
Reference
Synergism between halide binding and proton transport in a CLC-type exchanger., Accardi A, Lobet S, Williams C, Miller C, Dutzler R, J Mol Biol. 2006 Sep 29;362(4):691-9. Epub 2006 Aug 2. PMID:16949616
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