1mm0 | pdb_00001mm0

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

spinqualitylabelsall models 1mm0, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mm0 is a 1 chain structure with sequence from Pseus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TERN_PSEUS] Weak activity against Gram-positive bacteria B.megaterium, S.pyogenes and M.luteus, strong activity against yeasts C.albicans, C.neoformans and S.cerevisiae and filamentous fungi F.oxysporum, F.culmorum, N.crassa and N.hematococca. Less active against filamentous fungus T.viride. Inactive against Gram-positive bacteria A.viridans and S.aureus, filamentous fungi A.fumigatus and B.bassiana and yeast C.glabrata. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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.] Solution structure of termicin, an antimicrobial peptide from the termite Pseudacanthotermes spiniger.,Da Silva P, Jouvensal L, Lamberty M, Bulet P, Caille A, Vovelle F Protein Sci. 2003 Mar;12(3):438-46. PMID:12592014 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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