Complete resonance assignment of the first and second apple domains of MIC4 from Toxoplasma gondii, using a new NMRView-based assignment aid

Marchant, Jan; Sawmynaden, Kovilen; Saouros, Savvas; Simpson, Peter; Matthews, Stephen

doi:10.1007/s12104-008-9100-1

Cited by 34 publications

(31 citation statements)

References 10 publications

(8 reference statements)

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“…NMR Spectroscopy and Structure Calculation-Backbone and side chain assignments were completed using modified NMRview and standard triple-resonance assignment (18). NMR spectra were collected at 298 K on Bruker DRX500 and DRX800 spectrometers equipped with z-shielded gradient tripe resonance cryoprobes.…”

Section: Methodsmentioning

confidence: 99%

Structural Basis of Toxoplasma gondii MIC2-associated Protein Interaction with MIC2

Huynh

Liu

Henry

et al. 2015

Journal of Biological Chemistry

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Background: M2AP and the adhesin MIC2 form a complex involved in T. gondii gliding motility and invasion. Results: M2AP adopts a galectin-like fold featuring a hydrophobic ligand binding site required for association with MIC2. Conclusion: M2AP utilizes a modified galectin fold to bind a key adhesive protein.Significance: The galectin fold is adaptable for binding carbohydrate and protein substrates.

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Section: Methodsmentioning

confidence: 99%

Structural Basis of Toxoplasma gondii MIC2-associated Protein Interaction with MIC2

Huynh

Liu

Henry

et al. 2015

Journal of Biological Chemistry

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“…For both MNV VPg 11-85 and FCV VPg 9-79, the proteins used in structure determination and backbone and aliphatic side chain assignments were completed using an in-house NMRView-based assignment protocol (58). This was initially used in combination with MARS to establish sequential connectivity, after which assignments were completed (59).…”

Section: Methodsmentioning

confidence: 99%

Structures of the Compact Helical Core Domains of Feline Calicivirus and Murine Norovirus VPg Proteins

Leen

Kwok

Birtley

et al. 2013

J Virol

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fWe report the solution structures of the VPg proteins from feline calicivirus (FCV) and murine norovirus (MNV), which have been determined by nuclear magnetic resonance spectroscopy. In both cases, the core of the protein adopts a compact helical structure flanked by flexible N and C termini. Remarkably, while the core of FCV VPg contains a well-defined three-helix bundle, the MNV VPg core has just the first two of these secondary structure elements. In both cases, the VPg cores are stabilized by networks of hydrophobic and salt bridge interactions. The Tyr residue in VPg that is nucleotidylated by the viral NS7 polymerase (Y24 in FCV, Y26 in MNV) occurs in a conserved position within the first helix of the core. Intriguingly, given its structure, VPg would appear to be unable to bind to the viral polymerase so as to place this Tyr in the active site without a major conformation change to VPg or the polymerase. However, mutations that destabilized the VPg core either had no effect on or reduced both the ability of the protein to be nucleotidylated and virus infectivity and did not reveal a clear structure-activity relationship. The precise role of the calicivirus VPg core in virus replication remains to be determined, but knowledge of its structure will facilitate future investigations.

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“…The chemical shifts of 1 H N , 15 N, 13 C ␣ , 13 C ␤ , and 13 CЈ were obtained from the HNCACB/CBCA(CO)NH and HNCO/ HN(CA) CO experiments; the spectra were analyzed in NMRView, and assignments were made using a combination of the MARS automated assignment program (34) and an in-house assignment module (35 30.66 and 168.61 ms), and the NOE spectrum used a 1 H presaturation period of 5 s. T 1 and T 2 relaxation curves were fit to simple exponential functions using the rate analysis module in NMRView (33), and NOEs are reported as the ratio of intensities of the backbone amide peaks with and without 1 H presaturation. CPMG relaxation dispersion NMR experiments were performed at 14.1 and 18.8 T using the pulse sequences reported by Kay and co-workers (36).…”

Section: Methodsmentioning

confidence: 99%

Regulation of the Plasmodium Motor Complex

Douse

Green²,

Salgado

et al. 2012

Journal of Biological Chemistry

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Background: Recent phosphoproteome data reveal the extent of post-translational phosphorylation in selected apicomplexan parasites. Results: Binding site mutants that mimic the effect of MTIP phosphorylation in vivo severely decrease MyoA binding. Conclusion: Phosphorylation of selected binding site residues modulates the activity of the actomyosin motor. Significance: Study of Apicomplexa phosphosites can inform on the regulation of functions involved in pathogenesis.

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Complete resonance assignment of the first and second apple domains of MIC4 from Toxoplasma gondii, using a new NMRView-based assignment aid

Abstract: Microneme protein 4 is involved in cell binding by the important parasite Toxoplasma gondii. We present here the backbone and side-chain assignments of the first two apple domains together with a new graphical aid for their assignment using NMRView.

Cited by 34 publications

References 10 publications

Structural Basis of Toxoplasma gondii MIC2-associated Protein Interaction with MIC2

Structural Basis of Toxoplasma gondii MIC2-associated Protein Interaction with MIC2

Structures of the Compact Helical Core Domains of Feline Calicivirus and Murine Norovirus VPg Proteins

Regulation of the Plasmodium Motor Complex

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