ExbB: Difference between revisions

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<StructureSection load='5zfu' size='350' side='right' caption='2-isopropylmalate synthase complex with leucine, glycerol and Zn+2 ion (grey) (PDB code [[5zfu]])' scene=''>
[[Image:ExbB.jpg|300px|right|thumb| The Structure of ExbB<ref name='Kampfenkel'>PMID: 8449962</ref>]]
[[Image:ExbB.jpg|300px|right|thumb| The Structure of ExbB<ref name='Kampfenkel'>PMID: 8449962</ref>]]


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Loss of ExbB function can be partially replaced by TolQ and vice versa - reduced activities of either of these proteins via a mutant form can be reversed by introducing double mutants<ref name='Braun'>PMID: 15205446</ref>.
Loss of ExbB function can be partially replaced by TolQ and vice versa - reduced activities of either of these proteins via a mutant form can be reversed by introducing double mutants<ref name='Braun'>PMID: 15205446</ref>.
</StructureSection>
==3D structures of ExbB==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[5zfu]], [[5zfv]] – ExbD + ExbD peptide – ''Escherichia coli'' – Cryo EM<br />


== References==
== References==
<references/>
<references/>

Revision as of 10:33, 22 May 2018

The Structure of ExbB[1]

Structure

ExbB consists of three transmembrane domains (spanning from residues 16-39, 128-155 and 162-194), with two large portions of the protein representing the majority of the protein in the cytoplasm and two smaller portions in the periplasm[1].

ExbB can exist in the TonB system either in a complex with ExbD (to a ratio of 3.5:1) or on its own (where no ExbD is present), which has been suggested to play a part in the diverse roles of TonB[2].

ExbB has a similar sequence and physiological structure to TolQ and is therefore thought to be evolutionarily linked[3].

Function

ExbB is essential for TonB-dependent energy transduction as the absence of ExbB prevents TonB responding to the proton motive force, as well as the change of the high-affinity association of TonB for the outer membrane to the cytoplasmic membrane[2].

Loss of ExbB function can be partially replaced by TolQ and vice versa - reduced activities of either of these proteins via a mutant form can be reversed by introducing double mutants[3].

2-isopropylmalate synthase complex with leucine, glycerol and Zn+2 ion (grey) (PDB code 5zfu)

Drag the structure with the mouse to rotate

3D structures of ExbB3D structures of ExbB

Updated on 22-May-2018

5zfu, 5zfv – ExbD + ExbD peptide – Escherichia coli – Cryo EM

ReferencesReferences

  1. 1.0 1.1 Kampfenkel K, Braun V. Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli. J Biol Chem. 1993 Mar 15;268(8):6050-7. PMID:8449962
  2. 2.0 2.1 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
  3. 3.0 3.1 Braun V, Herrmann C. Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12. J Bacteriol. 2004 Jul;186(13):4402-6. PMID:15205446 doi:10.1128/JB.186.13.4402-4406.2004

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Laura McCauley, Michal Harel