6O4M
Racemic melittin
Summary for 6O4M
| Entry DOI | 10.2210/pdb6o4m/pdb |
| Descriptor | D-Melittin, Melittin, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | racemic, cytotoxic, antimicrobial, toxin |
| Biological source | Apis mellifera (Honeybee) More |
| Total number of polymer chains | 4 |
| Total formula weight | 12260.51 |
| Authors | Kurgan, K.W.,Bingman, C.A.,Gellman, S.H.,Forest, K.T. (deposition date: 2019-02-28, release date: 2019-05-22, Last modification date: 2024-11-06) |
| Primary citation | Kurgan, K.W.,Kleman, A.F.,Bingman, C.A.,Kreitler, D.F.,Weisblum, B.,Forest, K.T.,Gellman, S.H. Retention of Native Quaternary Structure in Racemic Melittin Crystals. J.Am.Chem.Soc., 141:7704-7708, 2019 Cited by PubMed Abstract: Racemic crystallography has been used to elucidate the secondary and tertiary structures of peptides and small proteins that are recalcitrant to conventional crystallization. It is unclear, however, whether racemic crystallography can capture native quaternary structure, which could be disrupted by heterochiral associations. We are exploring the use of racemic crystallography to characterize the self-assembly behavior of membrane-associated peptides, very few of which have been crystallized. We report a racemic crystal structure of the membrane-active peptide melittin; the new structure allows comparison with a previously reported crystal structure of L-melittin. The tetrameric assembly observed in crystalline L-melittin has been proposed to represent the tetrameric state detected in solution for this peptide. This tetrameric assembly is precisely reproduced in the racemic crystal, which strengthens the conclusion that the tetramer is biologically relevant. More broadly, these findings suggest that racemic crystallography can provide insight on native quaternary structure. PubMed: 31059253DOI: 10.1021/jacs.9b02691 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.27 Å) |
Structure validation
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