1mm0: Difference between revisions

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

OverviewOverview

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.]

About this StructureAbout this Structure

1MM0 is a Single protein structure of sequence from Pseudacanthotermes spiniger. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 13:56:33 2008

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OCA

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-[[Image:1mm0.gif|left|200px]]<br /><applet load="1mm0" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1mm0" />
 '''Solution structure of termicin, an antimicrobial peptide from the termite Pseudacanthotermes spiniger'''<br />
 ==Overview==
-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.]
+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.]
 ==About this Structure==
-MM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudacanthotermes_spiniger Pseudacanthotermes spiniger]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MM0 OCA].
+MM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudacanthotermes_spiniger Pseudacanthotermes spiniger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MM0 OCA].
 ==Reference==
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 [[Category: Jouvensal, L.]]
 [[Category: Lamberty, M.]]
-[[Category: Silva, P.Da.]]
+[[Category: Silva, P Da.]]
 [[Category: Vovelle, F.]]
 [[Category: antimicrobial peptide]]
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 [[Category: termite]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:31:11 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:33 2008''