1tkq
From Proteopedia
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| - | [[Image:1tkq.gif|left|200px]] | + | [[Image:1tkq.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF A LINKED UNSYMMETRIC GRAMICIDIN IN A MEMBRANE-ISOELECTRICAL SOLVENTS MIXTURE IN THE PRESENCE OF CsCl''' | + | {{Structure |
| + | |PDB= 1tkq |SIZE=350|CAPTION= <scene name='initialview01'>1tkq</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF A LINKED UNSYMMETRIC GRAMICIDIN IN A MEMBRANE-ISOELECTRICAL SOLVENTS MIXTURE IN THE PRESENCE OF CsCl''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TKQ is a [ | + | 1TKQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TKQ OCA]. |
==Reference== | ==Reference== | ||
| - | An asymmetric ion channel derived from gramicidin A. Synthesis, function and NMR structure., Xie X, Al-Momani L, Reiss P, Griesinger C, Koert U, FEBS J. 2005 Feb;272(4):975-86. PMID:[http:// | + | An asymmetric ion channel derived from gramicidin A. Synthesis, function and NMR structure., Xie X, Al-Momani L, Reiss P, Griesinger C, Koert U, FEBS J. 2005 Feb;272(4):975-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15691331 15691331] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Al-Momani, L.]] | [[Category: Al-Momani, L.]] | ||
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[[Category: beta-helix]] | [[Category: beta-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:19:40 2008'' |
Revision as of 12:19, 20 March 2008
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SOLUTION STRUCTURE OF A LINKED UNSYMMETRIC GRAMICIDIN IN A MEMBRANE-ISOELECTRICAL SOLVENTS MIXTURE IN THE PRESENCE OF CsCl
Overview
The biological ion channel gramicidin A (gA) was modified by synthetic means to obtain the tail-to-tail linked asymmetric gA-derived dimer compound 3. Single-channel current measurements for 3 in planar lipid bilayers exhibit an Eisenman I ion selectivity for alkali cations. The structural asymmetry does not lead to an observable functional asymmetry. The structure of 3 in solution without and with Cs cations was investigated by 1H-NMR spectroscopy. In CDCl3/CD3OH (1 : 1, v/v), 3 forms a mixture of double-stranded beta-helices. Upon addition of excess CsCl, the double-stranded species are converted completely into one new conformer: the right-handed single-stranded beta-helix. A combination of DQF-COSY and TOCSY was used for the assignment of the 1H-NMR spectrum of the Cs-3 complex in CDCl3/CD3OH (1 : 1, v/v). A total of 69 backbone, 27 long-range, and 64 side-chain distance restraints were obtained from NOESY together with 25 phi and 14 chi1 torsion angles obtained from coupling constants. These data were used as input for structure calculation with dyana built in sybyl 6.8. A final set of 11 structures with an average rmsd for the backbone of 0.45 A was obtained (PDB: 1TKQ). The structure of the Cs-3 complex in solution is equivalent to the bioactive channel conformation in the membrane environment.
About this Structure
1TKQ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
An asymmetric ion channel derived from gramicidin A. Synthesis, function and NMR structure., Xie X, Al-Momani L, Reiss P, Griesinger C, Koert U, FEBS J. 2005 Feb;272(4):975-86. PMID:15691331
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