2JR8
Solution structure of Manduca sexta moricin
Summary for 2JR8
| Entry DOI | 10.2210/pdb2jr8/pdb |
| NMR Information | BMRB: 15323 |
| Descriptor | Antimicrobial peptide moricin (1 entity in total) |
| Functional Keywords | antimicrobial peptide, antimicrobial protein |
| Total number of polymer chains | 1 |
| Total formula weight | 4551.54 |
| Authors | Gong, Y.,Dai, H.,Rayaprolu, S.,Huang, R.,Prakash, O.,Jiang, H. (deposition date: 2007-06-21, release date: 2008-03-25, Last modification date: 2024-05-08) |
| Primary citation | Dai, H.,Rayaprolu, S.,Gong, Y.,Huang, R.,Prakash, O.,Jiang, H. Solution structure, antibacterial activity, and expression profile of Manduca sexta moricin. J.Pept.Sci., 14:855-863, 2008 Cited by PubMed Abstract: In response to wounding or infection, insects produce a battery of antimicrobial peptides (AMPs) and other defense molecules to kill the invading pathogens. To study their structures, functions, and transcriptional regulation, we synthesized Manduca sexta moricin, a 42-residue peptide (GKIPVKAIKQAGKVIGKGLRAINIAGTTHDVVSFFRPKKKKH, 4539 Da). The compound exhibited potent antimicrobial activities against a broad spectrum of Gram-positive and Gram-negative bacteria with a minimum inhibitory concentration of 1.4 microM. The mRNA levels of M. sexta moricin increased substantially in fat body and hemocytes after the larvae were challenged with bacterial cells. We determined the solution structure of this AMP by two-dimensional 1H-1H -nuclear magnetic resonance spectroscopy. The tertiary structure is composed of an eight-turn alpha-helix spanning almost the entire peptide. Insights of relationships between the structure and function are also presented. PubMed: 18265434DOI: 10.1002/psc.1016 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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