Difference between revisions of "Part:BBa K554007"
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==Three-dimensional structure representation == | ==Three-dimensional structure representation == | ||
| − | You can find below a tridimensional structure of ATP-binding domain of hemolysin B from ''Escherichia coli'' (retrieved from PDB 1MT0 (Schmitt et al. 2003)) solved by crystallography and X-ray diffraction at 2.5 A resolution. This is a jmol applet, in which you can interactively see the protein structure of HlyB: | + | You can find below a tridimensional structure of ATP-binding domain of hemolysin B from ''Escherichia coli'' (retrieved from PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=1mt0 1MT0] (Schmitt et al. 2003)) solved by crystallography and X-ray diffraction at 2.5 A resolution. This is a jmol applet, in which you can interactively see the protein structure of HlyB: |
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Revision as of 12:47, 27 September 2011
Hemolysin B - HlyB
HlyB is part of the hemolysin secretion system ([http://2011.igem.org/Team:UNICAMP-EMSE_Brazil/Project#Device_3:_Secretion_system Device 3, Protein Secretion System]), very important to export the proteins produced inside bacteria and that must act in targets outside (such as IL-12 and IL-10). HlyB acts as a ATP-binding cassette, and recognizes the substrate via its secretion signal (like HlyA) and is responsible for the specificity of the secretion system process. This system is composed of 4 essential parts: the C-terminal signal sequence of alpha-hemolysin (HlyA, which will be linked to the export target protein), the two specific translocator proteins HlyB and HlyD and the outer membrane protein [BBa_K554009 TolC].
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 1301
Illegal BglII site found at 1964 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 231
- 1000COMPATIBLE WITH RFC[1000]
Usage and Biology
You can see a representation of this device acting in the schema below: HlyB gene and product are shown as a symbolic cilinder in orange.
Representation of device 3, the protein secretion system, in a Jedi bacteria that contains Device 1 (Adrenaline sensor/IL-12 producer). To export a protein, the bacteria must have the HlyD, HlyB and TolC proteins and the target protein must have a signal sequence (HlyA tail). In this case, the target protein to be secreted is IL-12.
A more realistic schema of ABC transport system is shown below:
Three-dimensional structure representation
You can find below a tridimensional structure of ATP-binding domain of hemolysin B from Escherichia coli (retrieved from PDB [http://www.pdb.org/pdb/explore/explore.do?structureId=1mt0 1MT0] (Schmitt et al. 2003)) solved by crystallography and X-ray diffraction at 2.5 A resolution. This is a jmol applet, in which you can interactively see the protein structure of HlyB:
References
Barbara D. Tzschaschel, Carlos A. Guzmán,, Kenneth N. Timmis and Victor de Lorenzo. An Escherichia coli hemolysin transport system-based vector for the export of polypeptides: Export of shiga-like toxin IIeB subunit by Salmonella typhimurium aroA. Nature Biotechnology 14, 765 - 769 (1996) [http://www.nature.com/nbt/journal/v14/n6/abs/nbt0696-765.html Article link]
P. Delepelaire. Type I secretion in Gram-negative bacteria. Biochimia et Biophysica Actca 1694, 149-161 (2004) [http://www.ncbi.nlm.nih.gov/pubmed/15546664 Link to PubMed]
Ivaylo Gentschev, Guido Dietrich and Werner Goebel. The E. coli α-hemolysin secretion system and its use in vaccine development. Trends in Microbiology 10, 39-45 (2002) [www.ncbi.nlm.nih.gov/pubmed/11755084 Link to PubMed]
Schmitt, L., Benabdelhak, H., Blight, M.A., Holland, I.B., Stubbs, M.T.Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains.Journal: (2003) J.Mol.Biol. 330: 333-342 [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=12823972 Link to PubMed]