|
|
| (5 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==F1-Gramicidin C In Sodium Dodecyl Sulfate Micelles (NMR)== | | ==F1-Gramicidin C In Sodium Dodecyl Sulfate Micelles (NMR)== |
| - | <StructureSection load='1nt6' size='340' side='right' caption='[[1nt6]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1nt6' size='340' side='right'caption='[[1nt6]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1nt6]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NT6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1nt6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_brevis Brevibacillus brevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NT6 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=QPH:N-FORMYL-L-PHENYLALANINE'>QPH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tk2|1tk2]], [[2xdc|2xdc]], [[1av2|1av2]], [[1bdw|1bdw]], [[1c4d|1c4d]], [[1gmk|1gmk]], [[1grm|1grm]], [[1jno|1jno]], [[1kqe|1kqe]], [[1mag|1mag]], [[1mic|1mic]], [[1ng8|1ng8]], [[1nrm|1nrm]], [[1nru|1nru]], [[1nt5|1nt5]], [[1jo3|1jo3]], [[1jo4|1jo4]], [[1tkq|1tkq]], [[1w5u|1w5u]], [[2izq|2izq]], [[3l8l|3l8l]], [[1al4|1al4]], [[1alx|1alx]], [[1alz|1alz]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=PRD_001128:mutant+GRAMICIDIN+C'>PRD_001128</scene>, <scene name='pdbligand=QPH:N-FORMYL-L-PHENYLALANINE'>QPH</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nt6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nt6 RCSB], [http://www.ebi.ac.uk/pdbsum/1nt6 PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nt6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nt6 OCA], [https://pdbe.org/1nt6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nt6 RCSB], [https://www.ebi.ac.uk/pdbsum/1nt6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nt6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 15: |
Line 16: |
| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 1nt6" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| Line 22: |
Line 24: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fletcher, T G]] | + | [[Category: Brevibacillus brevis]] |
| - | [[Category: Hinton, J F]] | + | [[Category: Large Structures]] |
| - | [[Category: Townsley, L E]] | + | [[Category: Fletcher TG]] |
| - | [[Category: Antibacterial]] | + | [[Category: Hinton JF]] |
| - | [[Category: Antibiotic]] | + | [[Category: Townsley LE]] |
| - | [[Category: Antifungal]]
| + | |
| - | [[Category: Gramicidin]]
| + | |
| - | [[Category: Linear gramicidin]]
| + | |
| - | [[Category: Membrane ion channel]]
| + | |
| - | [[Category: Sds micelle]]
| + | |
| Structural highlights
Publication Abstract from PubMed
To further investigate the effect of single amino acid substitution on the structure and function of the gramicidin channel, an analogue of gramicidin A (GA) has been synthesized in which Trp(15) is replaced by Gly in the critical aqueous interface and cation binding region. The structure of Gly(15)-GA incorporated into SDS micelles has been determined using a combination of 2D-NMR spectroscopy and molecular modeling. Like the parent GA, Gly(15)-GA forms a dimeric channel composed of two single-stranded, right-handed beta(6.3)-helices joined by hydrogen bonds between their N-termini. The replacement of Trp(15) by Gly does not have a significant effect on backbone structure or side chain conformations with the exception of Trp(11) in which the indole ring is rotated away from the channel axis. Measurement of the equilibrium binding constants and Delta G for the binding of monovalent cations to GA and Gly(15)-GA channels incorporated into PC vesicles using (205)Tl NMR spectroscopy shows that monovalent cations bind much more weakly to the Gly(15)-GA channel entrance than to GA channels. Utilizing the magnetization inversion transfer NMR technique, the transport of Na(+) ions through GA and Gly(15)-GA channels incorporated into PC/PG vesicles has been investigated. The Gly(15) substitution produces an increase in the activation enthalpy of transport and thus a significant decrease in the transport rate of the Na(+) ion is observed. The single-channel appearances show that the conducting channels have a single, well-defined structure. Consistent with the NMR results, the single-channel conductances are reduced by 30% and the lifetimes by 70%. It is concluded that the decrease in cation binding, transport, and conductance in Gly(15)-GA results from the removal of the Trp(15) dipole and, to a lesser extent, the change in orientation of Trp(11).
The structure, cation binding, transport, and conductance of Gly15-gramicidin A incorporated into SDS micelles and PC/PG vesicles.,Sham SS, Shobana S, Townsley LE, Jordan JB, Fernandez JQ, Andersen OS, Greathouse DV, Hinton JF Biochemistry. 2003 Feb 18;42(6):1401-9. PMID:12578352[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sham SS, Shobana S, Townsley LE, Jordan JB, Fernandez JQ, Andersen OS, Greathouse DV, Hinton JF. The structure, cation binding, transport, and conductance of Gly15-gramicidin A incorporated into SDS micelles and PC/PG vesicles. Biochemistry. 2003 Feb 18;42(6):1401-9. PMID:12578352 doi:10.1021/bi0204286
|
