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[[Image:1jno.jpg|left|200px]]
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{{STRUCTURE_1jno|  PDB=1jno  |  SCENE=  }}
'''Gramicidin A in Sodium Dodecyl Sulfate Micelles (NMR)'''


==Gramicidin A in Sodium Dodecyl Sulfate Micelles (NMR)==
<StructureSection load='1jno' size='340' side='right'caption='[[1jno]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jno]] 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=1JNO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JNO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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></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=1jno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jno OCA], [https://pdbe.org/1jno PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jno RCSB], [https://www.ebi.ac.uk/pdbsum/1jno PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jno ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Gramicidins 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.


==Overview==
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<ref>PMID:11570868</ref>
Gramicidins 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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNO OCA].
</div>
<div class="pdbe-citations 1jno" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11570868 11570868]
*[[Gramicidin|Gramicidin]]
[[Category: Hinton, J F.]]
== References ==
[[Category: Sham, S.]]
<references/>
[[Category: Townsley, L E.]]
__TOC__
[[Category: Tucker, W A.]]
</StructureSection>
[[Category: Beta-6 3 helix]]
[[Category: Brevibacillus brevis]]
[[Category: Linear gramicidin]]
[[Category: Large Structures]]
[[Category: Membrane ion channel]]
[[Category: Hinton JF]]
[[Category: Peptide antibiotic]]
[[Category: Sham S]]
[[Category: Right handed]]
[[Category: Townsley LE]]
[[Category: Sds micelle]]
[[Category: Tucker WA]]
[[Category: Single stranded helical dimer]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:27:56 2008''
Retrieved from "https://proteopedia.org/1jno"