3E7R
X-ray Crystal Structure of Racemic Plectasin
Summary for 3E7R
| Entry DOI | 10.2210/pdb3e7r/pdb |
| Related | 3E7U |
| Descriptor | Plectasin (2 entities in total) |
| Functional Keywords | plectasin, racemic protein crystallography, antibiotic, antimicrobial, cleavage on pair of basic residues, defensin, secreted, antimicrobial protein |
| Cellular location | Secreted (Probable): Q53I06 |
| Total number of polymer chains | 1 |
| Total formula weight | 4415.02 |
| Authors | Mandal, K.,Pentelute, B.L.,Tereshko, V.,Kossiakoff, A.A.,Kent, S.B.H. (deposition date: 2008-08-18, release date: 2009-06-09, Last modification date: 2024-10-16) |
| Primary citation | Mandal, K.,Pentelute, B.L.,Tereshko, V.,Thammavongsa, V.,Schneewind, O.,Kossiakoff, A.A.,Kent, S.B. Racemic crystallography of synthetic protein enantiomers used to determine the X-ray structure of plectasin by direct methods Protein Sci., 18:1146-1154, 2009 Cited by PubMed Abstract: We describe the use of racemic crystallography to determine the X-ray structure of the natural product plectasin, a potent antimicrobial protein recently isolated from fungus. The protein enantiomers L-plectasin and D-plectasin were prepared by total chemical synthesis; interestingly, L-plectasin showed the expected antimicrobial activity, while D-plectasin was devoid of such activity. The mirror image proteins were then used for racemic crystallization. Synchrotron X-ray diffraction data were collected to atomic resolution from a racemic plectasin crystal; the racemate crystallized in the achiral centrosymmetric space group P1 with one L-plectasin molecule and one D-plectasin molecule forming the unit cell. Dimer-like intermolecular interactions between the protein enantiomers were observed, which may account for the observed extremely low solvent content (13%-15%) and more highly ordered nature of the racemic crystals. The structure of the plectasin molecule was well defined for all 40 amino acids and was generally similar to the previously determined NMR structure, suggesting minimal impact of the crystal packing on the plectasin conformation. PubMed: 19472324DOI: 10.1002/pro.127 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1 Å) |
Structure validation
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