[NMR paper] Solution NMR Structures of Active Pyrenophora tritici-repentis ToxB and its Inactive Homolog Reveal Potential Determinants of Toxin Activity.
Related ArticlesSolution NMR Structures of Active Pyrenophora tritici-repentis ToxB and its Inactive Homolog Reveal Potential Determinants of Toxin Activity.
J Biol Chem. 2014 Jul 26;
Authors: Nyarko A, Singarapu KK, Figueroa M, Manning VA, Pandelova I, Wolpert TJ, Ciuffetti LM, Barbar E
Abstract
Ptr ToxB (ToxB) is a proteinaceous host-selective toxin produced by Pyrenophora tritici-repentis (Ptr), a plant pathogenic fungus that causes the disease tan spot of wheat. One feature that distinguishes ToxB from other host-selective toxins is that it has naturally occurring homologs in non-pathogenic Ptr isolates that lack toxic activity. There are no high-resolution structures for any of the ToxB homologs, or for any protein with greater than 30% sequence identity, and therefore what underlies activity remains an open question. Here we present the NMR structures of ToxB and its inactive homolog toxb. Both proteins adopt a ?-sandwich fold comprising three strands in each half that are bridged together by two disulfide bonds. The inactive toxb, however, shows higher flexibility localized to the sequence-divergent ?-sandwich half. The absence of toxic activity is attributed to a more open structure in the vicinity of one disulfide bond, higher flexibility, and residue differences in an exposed loop that likely impacts interaction with putative targets. We propose that activity is regulated by perturbations in a putative active site loop and changes in dynamics distant from the site of activity. Interestingly, the new structures identify AvrPiz-t, a secreted avirulence protein produced by the rice blast fungus, as a structural homolog to ToxB. This homology suggests that fungal proteins involved in either disease susceptibility such as ToxB or resistance such as AvrPiz-t may have a common evolutionary origin.
PMID: 25063993 [PubMed - as supplied by publisher]
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Biochemistry. 2011 Mar 30;
Authors: Piserchio A, Warthaka M, Devkota AK, Kaoud TS, Lee S, Abramczyk O, Ren P, Dalby KN, Ghose R
The mitogen activated protein (MAP) kinase ERK2 contains recruitment sites that engage canonical and non-canonical motifs found in a variety of upstream kinases, regulating phosphatases and downstream targets. Interactions involving two of these sites, the D-recruitment site...
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NMR solution structure of a cyanovirin homolog from wheat head blight fungus.
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Proteins. 2011 Jan 18;
Authors: Matei E, Louis JM, Jee J, Gronenborn AM
Members of the cyanovirin-N homolog (CVNH) lectin family are found in bacteria, fungi and plants. As part of our ongoing work on CVNH structure-function studies, we determined the high-resolution NMR solution structure of the homolog from the wheat head blight disease causing ascomycetous fungus Gibberella zeae (or Fusarium...
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Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
J Struct Funct Genomics. 2010 Dec 14;
Authors: Mani R, Vorobiev S, Swapna GV, Neely H, Janjua H, Ciccosanti C, Xiao R, Acton TB, Everett JK, Hunt J, Montelione GT
The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the Northeast Structural...
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12-15-2010 12:03 PM
[NMR paper] Ring current effects in the active site of medium-chain Acyl-CoA dehydrogenase reveal
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Medium-chain acyl-CoA dehydrogenase (MCAD) catalyzes the flavin-dependent oxidation of fatty acyl-CoAs to the corresponding trans-2-enoyl-CoAs. The interaction of hexadienoyl-CoA (HD-CoA), a product analogue, with recombinant pig...
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[NMR paper] Three-dimensional structure of the RGD-containing snake toxin albolabrin in solution,
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[NMR paper] Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of HIV-1 studied by 1H NMR.
J Mol Biol. 1994 Jan 7;235(1):287-301
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[NMR paper] Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of
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http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Conformational behaviour of the active and inactive forms of the nucleocapsid NCp7 of HIV-1 studied by 1H NMR.
J Mol Biol. 1994 Jan 7;235(1):287-301
Authors: Morellet N, de Rocquigny H, Mély Y, Jullian N, Déméné H, Ottmann M, Gérard D, Darlix JL, Fournie-Zaluski MC, Roques BP
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Solution NMR Structures of Active Pyrenophora tritici-repentis ToxB and its Inactive Homolog Reveal Potential Determinants of Toxin Activity.
Linear Mode
