1DLZ
SOLUTION STRUCTURE OF THE CHANNEL-FORMER ZERVAMICIN IIB (PEPTAIBOL ANTIBIOTIC)
Summary for 1DLZ
| Entry DOI | 10.2210/pdb1dlz/pdb |
| Related | 1AMT 1EE7 1GQ0 1IH9 1JOH 1M24 1OB4 1OB6 1OB7 1R9U |
| NMR Information | BMRB: 4601 |
| Related PRD ID | PRD_000159 |
| Descriptor | ZERVAMICIN IIB (1 entity in total) |
| Functional Keywords | zrevamicin, peptaibol, antibacterial, antifungal, antibiotic, bent helix |
| Biological source | EMERICELLOPSIS SALMOSYNNEMATA |
| Total number of polymer chains | 1 |
| Total formula weight | 1823.18 |
| Authors | Balashova, T.A.,Shenkarev, Z.O.,Tagaev, A.A.,Ovchinnikova, T.V.,Raap, J.,Arseniev, A.S. (deposition date: 1999-12-13, release date: 2000-02-03, Last modification date: 2025-03-26) |
| Primary citation | Balashova, T.A.,Shenkarev, Z.O.,Tagaev, A.A.,Ovchinnikova, T.V.,Raap, J.,Arseniev, A.S. NMR Structure of the Channel-Former Zervamicin Iib in Isotropic Solvents. FEBS Lett., 466:333-, 2000 Cited by PubMed Abstract: Spatial structure of the membrane channel-forming hexadecapeptide, zervamicin IIB, was studied by NMR spectroscopy in mixed solvents of different polarity ranging from CDCl3/CD3OH (9:1, v/v) to CD3OH/H2O (1:1, v/v). The results show that in all solvents used the peptide has a very similar structure that is a bent amphiphilic helix with a mean backbone root mean square deviation (rmsd) value of ca. 0.3 A. Side chains of Trp1, Ile2, Gln3, Ile5 and Thr6 are mobile. The results are discussed in relation to the validity of the obtained structure to serve as a building block of zervamicin IIB ion channels. PubMed: 10682854DOI: 10.1016/S0014-5793(99)01707-X PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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