Hydrogen gas-evolving membrane-bound hydrogenase (MBH) is a respiratory complex homologous to the quinone-reducing Complex I. Like Complex I, MBH has peripheral and membrane arms. MBH is made of 14 subunits (MbhA-N). MbhJ, K, L, N and M form the Membrane-anchored hydrogenase module. MbhJ, K, L, N are predicted to be exposed to the cytoplasm and form the peripheral arm. The remaining 10 subunits are predicted to be integral membrane proteins forming the membrane arm, made of 44 transmembrane helices (TMH) [2, 3]. MbhA, B, C and F form the Sodium translocation module. MbhD, E, G and H form the Proton translocation module. MbhI is the linker between the hydrogenase module and the proton-translocating membrane module. It anchors the discontinuous TMH7 of MbhH via its middle lateral helix and the C-terminal of TMH2, found in MbhE. MbhD and MbhE together are equivalent to Nqo10 of Complex I [1]. MbhD has three TM helices. Paper describing PDB structure 6cfw. [1]. 29754813. Structure of an Ancient Respiratory System.. Yu H, Wu CH, Schut GJ, Haja DK, Zhao G, Peters JW, Adams MWW, Li. H;. Cell. 2018;173:1636-1649.. [2]. 33229520. Structure of the Dietzia Mrp complex reveals molecular mechanism. of this giant bacterial sodium proton pump.. Li B, Zhang K, Nie Y, Wang X, Zhao Y, Zhang XC, Wu XL;. Proc Natl Acad Sci U S A. 2020;117:31166-31176.. [3]. 32735215. Structure and mechanism of the Mrp complex, an ancient. cation/proton antiporter.. Steiner J, Sazanov L;. Elife. 2020; [Epub ahead of print] (from Pfam)
- Date:
- 2024-08-14