ExbD: Difference between revisions
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<StructureSection load='2pfu' size='350' side='right' scene='' caption=''> | |||
[[Image:ExbD.jpg|300px|left|thumb| The Structure of ExbD<ref name='Kampfenkel'>PMID: 1644779</ref>]] | [[Image:ExbD.jpg|300px|left|thumb| The Structure of ExbD<ref name='Kampfenkel'>PMID: 1644779</ref>]] | ||
==Structure== | ==Structure== | ||
ExbD has a single transmembrane domain, with residues 1 to 22 on the cytoplasmic side and 44 to 141 in the periplasm. Residues 23 to 43 are within the cytoplasmic membrane and it is in this region, from residues 18 to 43, that the only hydrophobic residues in ExbD can be found<ref name='Kampfenkel'>PMID: 1644779</ref>. | |||
'''ExbD''' has a single transmembrane domain, with residues 1 to 22 on the cytoplasmic side and 44 to 141 in the periplasm (''see'' 3D structure 2PFU). Residues 23 to 43 are within the cytoplasmic membrane and it is in this region, from residues 18 to 43, that the only hydrophobic residues in ExbD can be found<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>, therefore it can be assumed that these two proteins will have a similar arrangement of their sequences. | ExbD has been shown to be approximately 25% identical and 70% similar to the [[TolR]] sequence<ref name='Kampfenkel'>PMID: 1644779</ref>, therefore it can be assumed that these two proteins will have a similar arrangement of their sequences. | ||
==Function== | ==Function== | ||
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<ref>PMID: 12193634</ref>. 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<ref name='Braun'>PMID: 15205446</ref>. | 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<ref>PMID: 12193634</ref>. 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<ref name='Braun'>PMID: 15205446</ref>. | ||
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The activity of ExbD can be affected with mutations of the single charged amino acid (here D25N) which lies close to the transmembrane region. This can also be said of the other transmembrane proteins ExbB, TolQ and TolR. | The activity of ExbD can be affected with mutations of the single charged amino acid (here D25N) which lies close to the transmembrane region. This can also be said of the other transmembrane proteins ExbB, TolQ and TolR. | ||
</StructureSection> | |||
==3D structures of ExbD== | |||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | |||
[[2pfu]] – EcExbD periplasmic domain – ''Escherichia coli'' – NMR<br /> | |||
[[5sv1]] – EcExbD residues 1-49 + EcExbB<br /> | |||
[[6tyi]] – EcExbD + ExbB – Cryo EM<br /> | |||
[[8pek]] – SmExbD periplasmic domain 43-140 - ''Serratia marsescens'' - NMR<br /> | |||
[[8p9r]] – SmExbD periplasmic domain + TonB<br /> | |||
[[8vgc]], [[8vgd]] – SmExbD periplasmic domain + D-box peptide<br /> | |||
[[7ajq]] – SmExbD + ExbB - Cryo EM<br /> | |||
== References== | == References== | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | |||
Latest revision as of 10:11, 3 June 2025
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3D structures of ExbD
Updated on 03-June-2025
TolR – EcExbD periplasmic domain – Escherichia coli – NMR
ExbB – EcExbD residues 1-49 + EcExbB
TonB – EcExbD + ExbB – Cryo EM
TolQ – SmExbD periplasmic domain 43-140 - Serratia marsescens - NMR
8p9r – SmExbD periplasmic domain + TonB
8vgc, 8vgd – SmExbD periplasmic domain + D-box peptide
7ajq – SmExbD + ExbB - Cryo EM
