1jo3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jo3]] 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=1JO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JO3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1jo3]] 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=1JO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JO3 FirstGlance]. <br> | ||
</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=FVA:N-FORMYL-L-VALINE'>FVA</scene>, <scene name='pdbligand=PRD_000151:GRAMICIDIN+B'>PRD_000151</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='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=FVA:N-FORMYL-L-VALINE'>FVA</scene>, <scene name='pdbligand=PRD_000151:GRAMICIDIN+B'>PRD_000151</scene></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=1jo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jo3 OCA], [https://pdbe.org/1jo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jo3 RCSB], [https://www.ebi.ac.uk/pdbsum/1jo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jo3 ProSAT]</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=1jo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jo3 OCA], [https://pdbe.org/1jo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jo3 RCSB], [https://www.ebi.ac.uk/pdbsum/1jo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jo3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Revision as of 10:55, 15 November 2023
Gramicidin B in Sodium Dodecyl Sulfate Micelles (NMR)Gramicidin B in Sodium Dodecyl Sulfate Micelles (NMR)
Structural highlights
Publication Abstract from PubMedGramicidins A, B, and C are the three most abundant, naturally occurring analogues of this family of channel-forming antibiotic. GB and GC differ from the parent pentadecapeptide, GA, by single residue mutations, W11F and W11Y, respectively. Although these mutations occur in the cation binding region of the channel, they do not affect monovalent cation specificity, but are known to alter cation-binding affinities, thermodynamic parameters of cation binding, conductance and the activation energy for ion transport. The structures of all three analogues incorporated into deuterated sodium dodecyl sulfate micelles have been obtained using solution state 2D-NMR spectroscopy and molecular modeling. For the first time, a rigorous comparison of the 3D structures of these analogues reveals that the amino acid substitutions do not have a significant effect on backbone conformation, thus eliminating channel differences as the cause of variations in transport properties. Variable positions of methyl groups in valine and leucine residues have been linked to molecular motions and are not likely to affect ion flow through the channel. Thus, it is concluded that changes in the magnitude and orientation of the dipole moment at residue 11 are responsible for altering monovalent cation transport. Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles.,Townsley LE, Tucker WA, Sham S, Hinton JF Biochemistry. 2001 Oct 2;40(39):11676-86. PMID:11570868[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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