1jo3
From Proteopedia
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[[Image:1jo3.jpg|left|200px]] | [[Image:1jo3.jpg|left|200px]] | ||
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'''Gramicidin B in Sodium Dodecyl Sulfate Micelles (NMR)''' | '''Gramicidin B in Sodium Dodecyl Sulfate Micelles (NMR)''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JO3 OCA]. | |
==Reference== | ==Reference== | ||
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] | 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] | ||
| - | [[Category: Brevibacillus brevis]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Hinton, J F.]] | [[Category: Hinton, J F.]] | ||
[[Category: Townsley, L E.]] | [[Category: Townsley, L E.]] | ||
[[Category: Tucker, W A.]] | [[Category: Tucker, W A.]] | ||
| - | [[Category: | + | [[Category: Beta-6 3 helix]] |
| - | [[Category: | + | [[Category: Linear gramicidin]] |
| - | [[Category: | + | [[Category: Membrane ion channel]] |
| - | [[Category: | + | [[Category: Peptide antibiotic]] |
| - | [[Category: | + | [[Category: Right handed]] |
| - | [[Category: | + | [[Category: Sds micelle]] |
| - | [[Category: | + | [[Category: Single stranded helical dimer]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:29:20 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:29, 2 May 2008
Gramicidin B in Sodium Dodecyl Sulfate Micelles (NMR)
Overview
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
Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 21:29:20 2008
