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Fold of antiporter-like subunits

Two essential charged residues that are conserved from Mrp antiporters to complex I are found in TM5:
L(Glu 144),color magenta
; M(Glu 144), color blue ;N(Glu 133);color yellow;
In the middle of TM7: L(Lys 229),color red; M(Lys 234),color cyan; N(Lys 217),color green,
and its e-amino group points inside the putative proton channel.


Conserved polar residues in TM12:
L(Lys 399) color green, N(Lys 395) color red lies at the beginning of the periplasmic half of TM12. It may interact with, and stabilize, the negatively charged C terminus of TM12a.

Two discontinuous helices -TM7 and TM12 contain a proline that is conserved between all three antiporter-like subunits: M(Pro 239) in TM7 and M(Pro 399) in TM12;Such helices are likely to participate in proton or ion transport by introducing some flexibility and charge to the middle of the membrane.

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Structure of the membrane domain of respiratory complex I.

Efremov RG1Sazanov LA

  (PubMed)

3rko(PDB)