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We investigated OSCC cell lines from tissues with
EIIA was overexpressed, purified, crystallized and the structure solved as described above. The final model contains three dimers of E. faecalis EIIAgnt, covering residues 1–140 (chains B, D, E, F; chain A: 1–137, chain C: 1–139), 10 Ca2+ ions derived from the buffer and 149 water molecules. Residues 141–150 appear to be flexible in the crystals. EIIAgnt is present as a tightly interacting dimer in the crystal structure and consists of a four-stranded parallel β-sheet which is flanked by three helices on each side. In the dimer, both C-termini extend on top of the neighboring monomer and provide an additional strand to the central β-sheet in an antiparallel fashion ( Fig. 1a), ( Table 1). The interface between the monomers covers a surface area of about 1825 ?2 (24%), consists of 50 rather JNK-IN-8 residues and has 15 hydrogen bonds [25] which is in good accordance with average values for protein interfaces [33]. Considering size and nature of the protein–protein interface we suggest endoplasmic reticulum (ER) the observed homodimer is physiologically relevant, which was indicated for several other EIIA components as well [1], [6], [34] and [35]. The peptide backbone of EIIAgnt clearly resembles the typical fold of the mannose family EIIA components [2] and [15] and superposition with EIIAman from E. coli [6], [8] and [20] results in a root mean square deviation (RMSD) of 1.6 ? over 133 corresponding residues [24] while the sequence identity is only 24% [36]. Also the EIIAman active site residue His-10 which first receives and then donates the phosphoryl group during the transfer reactions [37] has with His-9 its counterpart in EIIAgnt ( Fig. 2).

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