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1MM0

Solution structure of termicin, an antimicrobial peptide from the termite Pseudacanthotermes spiniger

Summary for 1MM0
Entry DOI10.2210/pdb1mm0/pdb
DescriptorTermicin (1 entity in total)
Functional Keywordstermite, cytein-rich, antimicrobial peptide, insect defensin, csab motif, antimicrobial protein
Biological sourcePseudacanthotermes spiniger
Cellular locationSecreted: P82321
Total number of polymer chains1
Total formula weight4227.88
Authors
Da Silva, P.,Jouvensal, L.,Lamberty, M.,Bulet, P.,Caille, A.,Vovelle, F. (deposition date: 2002-09-02, release date: 2003-05-13, Last modification date: 2024-10-23)
Primary citationDa Silva, P.,Jouvensal, L.,Lamberty, M.,Bulet, P.,Caille, A.,Vovelle, F.
Solution structure of termicin, an antimicrobial peptide from the termite Pseudacanthotermes spiniger
PROTEIN SCI., 12:438-446, 2003
Cited by
PubMed Abstract: The solution structure of termicin from hemocytes of the termite Pseudacanthotermes spiniger was determined by proton two-dimensional nuclear magnetic resonance spectroscopy and molecular modeling techniques. Termicin is a cysteine-rich antifungal peptide also exhibiting a weak antibacterial activity. The global fold of termicin consists of an alpha-helical segment (Phe4-Gln14) and a two-stranded (Phe19-Asp25 and Gln28-Phe33) antiparallel beta-sheet forming a "cysteine stabilized alphabeta motif" (CSalphabeta) also found in antibacterial and antifungal defensins from insects and from plants. Interestingly, termicin shares more structural similarities with the antibacterial insect defensins and with MGD-1, a mussel defensin, than with the insect antifungal defensins such as drosomycin and heliomicin. These structural comparisons suggest that global fold alone does not explain the difference between antifungals and antibacterials. The antifungal properties of termicin may be related to its marked hydrophobicity and its amphipatic structure as compared to the antibacterial defensins. [SWISS-PROT accession number: Termicin (P82321); PDB accession number: 1MM0.]
PubMed: 12592014
DOI: 10.1110/ps.0228303
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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