2RQO
Solution structure of Polytheonamide B
Summary for 2RQO
| Entry DOI | 10.2210/pdb2rqo/pdb |
| Related PRD ID | PRD_000224 |
| Descriptor | polytheonamide B (1 entity in total) |
| Functional Keywords | beta-helix, toxin |
| Biological source | Theonella swinhoei |
| Total number of polymer chains | 1 |
| Total formula weight | 5033.76 |
| Authors | Hamada, N.,Matsunaga, S.,Fujiwara, M.,Fujjita, K.,Hirota, H.,Schmucki, R.,Guntert, P.,Fusetani, N. (deposition date: 2009-09-03, release date: 2010-09-15, Last modification date: 2023-11-15) |
| Primary citation | Hamada, T.,Matsunaga, S.,Fujiwara, M.,Fujita, K.,Hirota, H.,Schmucki, R.,Guntert, P.,Fusetani, N. Solution Structure of Polytheonamide B, a Highly Cytotoxic Nonribosomal Polypeptide from Marine Sponge J.Am.Chem.Soc., 2010 Cited by PubMed Abstract: Polytheonamide B (pTB), a highly cytotoxic polypeptide, is one of the most unusual nonribosomal peptides of sponge origin. pTB is a linear 48-residue peptide with alternating D- and L-amino acids and contains a total of eight types of nonproteinogenic amino acids. To investigate the mechanisms underlying its cytotoxic activity, we determined the three-dimensional structure of pTB by NMR spectroscopy, structure calculation, and energy minimization. pTB adopts a single right-handed β(6.3)-helical structure in a 1:1 mixture of methanol/chloroform with a length of approximately 45 A and a hydrophilic pore of ca. 4 A inner diameter. These features indicate that pTB molecules form transmembrane channels that permeate monovalent cations as gramicidin A channels do. The strong cytotoxicity of pTB can be ascribed to its ability to form single molecule channels through biological membranes. PubMed: 20795624DOI: 10.1021/ja104616z PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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