Difference between revisions of "Part:BBa K808001"

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tphC: terephtalate periplasmatic binding proteine of the tripartite transporter family

Figure 1. Homology modelling of tphC_322 with Phyre2 A-D A. The model of tphC_322 B. Crystal structure of bugT C. Crystal structure of bugD D. Crystal structure of bug27. Images coloured by rainbow N to C terminus.

Figure 1. Results of SignalP 4.0 Server prediction of tphC_322. TphC_322 has a signal peptide and a cleavage site between amino acid 26 and 27

The putative terephtalate periplasmatic binding proteine (tphC_322, 34,38 kDa) was isolated from Comamonas testosteroni KF-1. The strain was purchased from Leibniz Institute DMSZ-German Collection of Microorganism and Cell Cultures (DMSZ no. 14576). The original sequence contains a Pst1 recognition site.To eliminate this recognition site a directed-site mutagenic PCR was performed. (For more datails link zu dem PCR protokoll und dem Labjournal, wo isolations PCR beschrieben wird) To characterized the structure of the tphC_322 bioinformatic tools like Protein Homology/anologY Recognition Engine V 2.0 (Phyre2), SignalIP 4.0 Server and TatP 1.0 Server was used. The homology modelling of the tphC_322 with Phyre2 shows 35% identity with BugT (Fig. 1.B,PDB entry 2DVZ) , 31 % identity with transport protein bugD (Fig.1.C,PDB entry 2F5X) and 28 % identity with transport proten bug27 (Fig. 1.D,PDB entry 2QPQ). All this proteins play a role in the transport of small molecules into the cell of Bordetella pertussis and belong to the group of periplasmatic bindig proteins of the tripartite tricarboxylate family. The tripartite tricarboxylate transporter system consists of three different proteins: a periplasmatic solute binding receptor (in this case tphC_322), a membrane protein with 12 putative transmembrane alpha-helical spanners, and a small poorly conserved membrane proteine with four putative transmembrane alpha-helical spanners.^[1]The structure similarity (Fig.1 A-D) of the tphC_322 with BugT, BugD and Bug27 suggest that the tphC_322 also belongs to the tripartite tricarboxylate transporter family. SignalP 4.0 Server results show, that tphC_322 has a signal peptide and a cleavage site between amino acid 26 and 27.(Fig.3) The TatP 1.0 Server predicted no significant Twin-argenine signal peptide. (Data not shown). It´s suggest that the tphC_322 passes the inner membrane via the Sec protein-translocation pathway.

Sequence and Features

References

• [1] Sasoh, M., E. Masai, et al. (2006). "Characterization of the terephthalate degradation genes of Comamonas sp. strain E6." Appl Environ Microbiol 72(3): 1825-1832.