Summary for 1ALZ
| Entry DOI | 10.2210/pdb1alz/pdb |
| Related | 1AL4 1ALX 1AV2 1BDW 1C4D 1GMK 1GRM 1JNO 1JO3 1JO4 1KQE 1MAG 1MIC 1NG8 1NRM 1NRU 1NT5 1NT6 1TK2 1TKQ 1W5U 2IZQ 2XDC 3L8L |
| Related PRD ID | PRD_000150 PRD_000153 |
| Descriptor | ILE-GRAMICIDIN C, VAL-GRAMICIDIN A, ETHANOL, ... (4 entities in total) |
| Functional Keywords | gramicidin, antifungal, antibiotic, antibacterial, membrane ion channel, linear gramicidin |
| Biological source | BREVIBACILLUS BREVIS More |
| Total number of polymer chains | 2 |
| Total formula weight | 4400.53 |
| Authors | Burkhart, B.M.,Pangborn, W.A.,Duax, W.L.,Langs, D.A. (deposition date: 1997-06-06, release date: 1998-03-04, Last modification date: 2023-11-15) |
| Primary citation | Burkhart, B.M.,Gassman, R.M.,Langs, D.A.,Pangborn, W.A.,Duax, W.L. Heterodimer Formation and Crystal Nucleation of Gramicidin D Biophys.J., 75:2135-, 1998 Cited by PubMed Abstract: The linear pentadecapeptide antibiotic gramicidin D is a heterogeneous mixture of six components. Precise refinements of three-dimensional structures of naturally occurring gramicidin D in crystals obtained from methanol, ethanol, and n-propanol demonstrate the unexpected presence of stable left-handed antiparallel double-helical heterodimers that vary with the crystallization solvent. The side chains of Trp residues in the three structures exhibit sequence-specific patterns of conformational preference. Tyr substitution for Trp at position 11 appears to favor beta ribbon formation and stabilization of the antiparallel double helix that acts as a template for gramicidin folding and nucleation of different crystal forms. The fact that a minor component in a heterogeneous mixture influences aggregation and crystal nucleation has potential applications to other systems in which anomalous behavior is exhibited by aggregation of apparently homogeneous materials, such as the enigmatic behavior of prion proteins. PubMed: 9788907DOI: 10.1016/S0006-3495(98)77656-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.86 Å) |
Structure validation
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