PXD008247-1

PXD008247 is an original dataset announced via ProteomeXchange.

Title	High-resolution cryo-EM structure of the respiratory alternative complex III from Rhodothermus marinus
Description	Electron transfer in respiratory chains generates the electrochemical potential that serves as the energy source for ATP synthesis, solute transport and motility. In eukaryotes and many bacteria, the respiratory chain consists of four electron transport complexes, known as complex I to IV. Respiratory chains of some prokaryotes differ in composition and organization. They can use a wide range of electron donors and acceptors and may have complexes performing the same catalytic reaction. The diversity and apparent redundancy of prokaryotic respiratory chains reflects the versatility and robustness of the organisms. Many of these alternative respiratory chain complexes are either unknown or their structures and mechanisms remain elusive. In this work we describe a 3.9 A cryo-EM structure of the alternative complex III (ACIII) from Rhodothermus marinus, which we demonstrated takes over the role of canonical respiratory complex III (bc1 complex), even though it is structurally unrelated. Our structure reveals that ACIII is an integral membrane protein complex of at least 7 subunits (ActABCDEFH). The periplasmic domain, with ActA, B, E and H, harbours four iron-sulphur clusters and six C-type hemes. The cofactors form two electron wires that converge on the putative quinol-binding site in subunit ActC. The two homologous subunits, ActC and ActF, each have two four-helix bundles in the membrane, with several conserved polar residues that delineate putative proton channels. ACIII meets all requirements for an energy-transducing machine that couples electron transfer from quinol to the oxygen reductase, to translocation of protons across the membrane.
HostingRepository	PRIDE
AnnounceDate	2018-05-08
AnnouncementXML	Submission_2018-05-08_04:55:02.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Julian Langer
SpeciesList	scientific name: Rhodothermus marinus; NCBI TaxID: 29549;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	impact II

Revision	Datetime	Status	ChangeLog Entry
0	2017-11-20 07:25:59	ID requested
⏵ 1	2018-05-08 04:55:03	announced
2	2024-10-22 04:41:36	announced	2024-10-22: Updated project metadata.

Sousa JS, Calisto F, Langer JD, Mills DJ, Refojo PN, Teixeira M, K, ü, hlbrandt W, Vonck J, Pereira MM, Structural basis for energy transduction by respiratory alternative complex III. Nat Commun, 9(1):1728(2018) [pubmed]

curator keyword: Biological

submitter keyword: Complex III, cryo-EM, proteomics

Julian David Langer
contact affiliation	MPI of Biophysics and MPI for Brain Research
contact email	julian.langer@biophys.mpg.de
lab head
Julian Langer
contact affiliation	MPIs for Biophysics and Brain Research
contact email	julian.langer@biophys.mpg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD008247
     1. Label: PRIDE project
     2. Name: High-resolution cryo-EM structure of the respiratory alternative complex III from Rhodothermus marinus