Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
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SHR Neuro Krebs Kardio Lipid Stoffw Microb
Goessweiner-Mohr, N; Grumet, L; Pavkov-Keller, T; Birner-Gruenberger, R; Grohmann, E; Keller, W.
Crystallization and preliminary structure determination of the transfer protein TraM from the Gram-positive conjugative plasmid pIP501.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013; 69(Pt 2):178-183
Doi: 10.1107/S1744309113000134
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- Co-Autor*innen der Med Uni Graz
- Birner-Grünberger Ruth
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- Abstract:
- The major means of horizontal gene spread (e.g. of antibiotic resistance) is conjugative plasmid transfer. It presents a serious threat especially for hospitalized and immuno-suppressed patients, as it can lead to the accelerated spread of bacteria with multiple antibiotic resistances. Detailed information about the process is available only for bacteria of Gram-negative (G-) origin and little is known about the corresponding mechanisms in Gram-positive (G+) bacteria. Here we present the purification, biophysical characterization, crystallization and preliminary structure determination of the TraM C-terminal domain (TraMΔ, comprising residues 190-322 of the full-length protein), a putative transfer protein from the G+ conjugative model plasmid pIP501. The crystals diffracted to 2.5 Å resolution and belonged to space group P1, with unit-cell parameters a = 39.21, b = 54.98, c = 93.47 Å, α = 89.91, β = 86.44, γ = 78.63° and six molecules per asymmetric unit. The preliminary structure was solved by selenomethionine single-wavelength anomalous diffraction.
- Find related publications in this database (using NLM MeSH Indexing)
- Bacterial Proteins - chemistry
- Buffers -
- Chromatography, Gel -
- Circular Dichroism -
- Conjugation, Genetic -
- Crystallization -
- Crystallography, X-Ray -
- Electrophoresis, Polyacrylamide Gel -
- Gram-Positive Bacteria - metabolism
- Plasmids - metabolism
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization -