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-Structure paper
Title | Structure of an Ancient Respiratory System. |
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Journal, issue, pages | Cell, Vol. 173, Issue 7, Page 1636-1649.e16, Year 2018 |
Publish date | Jun 14, 2018 |
Authors | Hongjun Yu / Chang-Hao Wu / Gerrit J Schut / Dominik K Haja / Gongpu Zhao / John W Peters / Michael W W Adams / Huilin Li / |
PubMed Abstract | Hydrogen gas-evolving membrane-bound hydrogenase (MBH) and quinone-reducing complex I are homologous respiratory complexes with a common ancestor, but a structural basis for their evolutionary ...Hydrogen gas-evolving membrane-bound hydrogenase (MBH) and quinone-reducing complex I are homologous respiratory complexes with a common ancestor, but a structural basis for their evolutionary relationship is lacking. Here, we report the cryo-EM structure of a 14-subunit MBH from the hyperthermophile Pyrococcus furiosus. MBH contains a membrane-anchored hydrogenase module that is highly similar structurally to the quinone-binding Q-module of complex I while its membrane-embedded ion-translocation module can be divided into a H- and a Na-translocating unit. The H-translocating unit is rotated 180° in-membrane with respect to its counterpart in complex I, leading to distinctive architectures for the two respiratory systems despite their largely conserved proton-pumping mechanisms. The Na-translocating unit, absent in complex I, resembles that found in the Mrp H/Na antiporter and enables hydrogen gas evolution by MBH to establish a Na gradient for ATP synthesis near 100°C. MBH also provides insights into Mrp structure and evolution of MBH-based respiratory enzymes. |
External links | Cell / PubMed:29754813 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.7 Å |
Structure data | |
Chemicals | ChemComp-SF4: ChemComp-NFU: |
Source |
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Keywords | MEMBRANE PROTEIN / respiratory / hydrogenase / ion translocation |