1JNO
Gramicidin A in Sodium Dodecyl Sulfate Micelles (NMR)
Summary for 1JNO
| Entry DOI | 10.2210/pdb1jno/pdb |
| Related | 1AL4 1ALX 1ALZ 1AV2 1BDW 1C4D 1GMK 1GRM 1JO3 1JO4 1KQE 1MAG 1MIC 1NG8 1NRM 1NRU 1NT5 1NT6 1TK2 1TKQ 1W5U 2IZQ 2XDC 3L8L |
| Related PRD ID | PRD_000150 |
| Descriptor | GRAMICIDIN A (1 entity in total) |
| Functional Keywords | gramicidin, antifungal, antibacterial, sds micelles, membrane ion channel, linear gramicidin, antibiotic |
| Biological source | BREVIBACILLUS BREVIS |
| Total number of polymer chains | 2 |
| Total formula weight | 3764.59 |
| Authors | Tucker, W.A.,Sham, S.,Townsley, L.E.,Hinton, J.F. (deposition date: 2001-07-24, release date: 2001-08-08, Last modification date: 2024-11-20) |
| Primary citation | Townsley, L.E.,Tucker, W.A.,Sham, S.,Hinton, J.F. Structures of Gramicidins A, B, and C Incorporated Into Sodium Dodecyl Sulfate Micelles. Biochemistry, 40:11676-, 2001 Cited by PubMed Abstract: 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. PubMed: 11570868DOI: 10.1021/BI010942W PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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