ExbD
From Proteopedia
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[[Image:ExbD.jpg|300px|right|thumb| The Structure of ExbD<ref name='Kampfenkel'>PMID: 1644779</ref>]] | [[Image:ExbD.jpg|300px|right|thumb| The Structure of ExbD<ref name='Kampfenkel'>PMID: 1644779</ref>]] | ||
| + | ExbD has a single transmembrane domain, with residues 1 to 22 on the cytoplasmic side, 23 to 43 within the cytoplasmic membrane and 44 to 141in the periplasm.<ref name='Kampfenkel'>PMID: 1644779</ref> | ||
| + | ExbD has been shown to be approximately 25% identical and 70% similar to the [[TolR]] sequence<ref name='Kampfenkel'>PMID: 1644779</ref>, it can be assumed that these two proteins will have a similar arrangement of their sequences. It has also been shown that TolR can replace the function of an ExbD mutant just as [[TolQ]] can with ExbB, suggesting an evolutionary link between the two complexes. | ||
== References== | == References== | ||
<references/> | <references/> | ||
Revision as of 11:53, 14 February 2011
ExbD is present in cells only in a complex with ExbB, where is affects the functioning of the TonB complex both in how it responds to the proton motive force as well as its affinity with either the cytoplasmic or outer membrane. [1]
Structure
ExbD has a single transmembrane domain, with residues 1 to 22 on the cytoplasmic side, 23 to 43 within the cytoplasmic membrane and 44 to 141in the periplasm.[2]
ExbD has been shown to be approximately 25% identical and 70% similar to the TolR sequence[2], it can be assumed that these two proteins will have a similar arrangement of their sequences. It has also been shown that TolR can replace the function of an ExbD mutant just as TolQ can with ExbB, suggesting an evolutionary link between the two complexes.
References
- ↑ Held KG, Postle K. ExbB and ExbD do not function independently in TonB-dependent energy transduction. J Bacteriol. 2002 Sep;184(18):5170-3. PMID:12193634
- ↑ 2.0 2.1 2.2 Kampfenkel K, Braun V. Membrane topology of the Escherichia coli ExbD protein. J Bacteriol. 1992 Aug;174(16):5485-7. PMID:1644779
