Difference between revisions of "Part:BBa K259000"
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__NOTOC__ | __NOTOC__ | ||
<partinfo>BBa_K259000 short</partinfo> | <partinfo>BBa_K259000 short</partinfo> | ||
+ | |||
+ | ===Biology of fhuA=== | ||
fhuA is an outer membrane (OM) protein that is found in the gram negative bacterium, E.coli. It is involved in the active-transport (energy-dependent uptake) of ferrichrome-iron from the extracellular environment. However fhuA is only able to bind ferrichrome-iron (i.e. ferrichrome iron is a ligand of fhuA protein). For the uptake to be completed fhuA needs to form a complex with another protein, tonB that carries out the energy-dependent uptake by using ATP as substrate to undergo the relevant conformational changes. | fhuA is an outer membrane (OM) protein that is found in the gram negative bacterium, E.coli. It is involved in the active-transport (energy-dependent uptake) of ferrichrome-iron from the extracellular environment. However fhuA is only able to bind ferrichrome-iron (i.e. ferrichrome iron is a ligand of fhuA protein). For the uptake to be completed fhuA needs to form a complex with another protein, tonB that carries out the energy-dependent uptake by using ATP as substrate to undergo the relevant conformational changes. | ||
− | This biobrick | + | |
+ | ===What this Biobrick gives you upon expression=== | ||
+ | |||
+ | This biobrick encodes ONLY for fhuA. | ||
+ | |||
+ | ===fhuA Statistics=== | ||
fhuA is a beta-barell protein (22 anti-parallel beta-strands) and is composed of 747 aminoacids. This receptor protein may be used as an attachment point by some colicins. | fhuA is a beta-barell protein (22 anti-parallel beta-strands) and is composed of 747 aminoacids. This receptor protein may be used as an attachment point by some colicins. | ||
− | + | {| style="color:white; background-color:#0066CC;" cellpadding="20" cellspacing="0" border="2" | |
+ | !Chassis | ||
+ | !Monomer/Multimer | ||
+ | !Aminoacid Length/Weight | ||
+ | !Localisation | ||
+ | !Structure | ||
+ | |- | ||
+ | |E.Coli | ||
+ | |Monomer | ||
+ | |747/82.182kDa | ||
+ | |Outer Membrane | ||
+ | |beta-barrel | ||
+ | |} | ||
+ | |||
+ | |||
+ | ===References=== | ||
Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L., Rosenusch J.P. and Moras D. (1998),Transmembrane signalling across the Ligand-Gated FhuAReceptor: Crystal structures of Free and Ferrichrome-Bound States reveal allosteric changes. Cell 95,771-778. | Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L., Rosenusch J.P. and Moras D. (1998),Transmembrane signalling across the Ligand-Gated FhuAReceptor: Crystal structures of Free and Ferrichrome-Bound States reveal allosteric changes. Cell 95,771-778. | ||
− | Uniprot access number | + | [http://www.uniprot.org/uniprot/P06971 Uniprot access number P06971] |
− | + | [http://ecogene.org/geneInfo.php?eg_id=EG10302 EcoGene Access Number EG10302] | |
Revision as of 17:46, 14 July 2009
fhuA - Outer membrane transporter for ferrichrome-iron
Biology of fhuA
fhuA is an outer membrane (OM) protein that is found in the gram negative bacterium, E.coli. It is involved in the active-transport (energy-dependent uptake) of ferrichrome-iron from the extracellular environment. However fhuA is only able to bind ferrichrome-iron (i.e. ferrichrome iron is a ligand of fhuA protein). For the uptake to be completed fhuA needs to form a complex with another protein, tonB that carries out the energy-dependent uptake by using ATP as substrate to undergo the relevant conformational changes.
What this Biobrick gives you upon expression
This biobrick encodes ONLY for fhuA.
fhuA Statistics
fhuA is a beta-barell protein (22 anti-parallel beta-strands) and is composed of 747 aminoacids. This receptor protein may be used as an attachment point by some colicins.
Chassis | Monomer/Multimer | Aminoacid Length/Weight | Localisation | Structure |
---|---|---|---|---|
E.Coli | Monomer | 747/82.182kDa | Outer Membrane | beta-barrel |
References
Locher K.P., Rees B., Koebnik R., Mitschler A., Moulinier L., Rosenusch J.P. and Moras D. (1998),Transmembrane signalling across the Ligand-Gated FhuAReceptor: Crystal structures of Free and Ferrichrome-Bound States reveal allosteric changes. Cell 95,771-778.
[http://www.uniprot.org/uniprot/P06971 Uniprot access number P06971]
[http://ecogene.org/geneInfo.php?eg_id=EG10302 EcoGene Access Number EG10302]
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 682
Illegal AgeI site found at 820
Illegal AgeI site found at 1225
Illegal AgeI site found at 1999 - 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI.rc site found at 724