PDBsum entry 6hlm

Electron transport

PDB id: 6hlm

Contents

Protein chains

155 a.a.

416 a.a.

Ligands

FES ×2

SF4 ×2

FMN ×2

NAD ×2

MPO ×2

Metals

_NA

Waters ×497

PDB id:

6hlm

Name:

Electron transport

Title:

Variant g129d of nuoef from aquifex aeolicus bound to NAD+

Structure:

Nadh-quinone oxidoreductase subunit e. Chain: a, c. Synonym: nadh dehydrogenase i subunit e,ndh-1 subunit e. Engineered: yes. Mutation: yes. Other_details: g129d variant of nuoe. Nadh-quinone oxidoreductase subunit f. Chain: b, d. Synonym: nadh dehydrogenase i subunit f,ndh-1 subunit f.

Source:

Aquifex aeolicus. Organism_taxid: 63363. Gene: nuoe, aq_574. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: nuof, aq_573. Expression_system_taxid: 562

Resolution:

1.80Å R-factor: 0.177 R-free: 0.197

Authors:

S.Gerhardt,T.Friedrich,O.Einsle,E.Gnandt,M.Schulte,D.Fiegen

Key ref:

M.Schulte et al. (2019). A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I. Nat Commun, 10, 2551. PubMed id: 31186428 DOI: 10.1038/s41467-019-10429-0

Date:

11-Sep-18 Release date: 26-Jun-19

Protein chains

O66842  (NUOE_AQUAE) -  NADH-quinone oxidoreductase subunit E from Aquifex aeolicus (strain VF5)

Seq: 160 a.a.

Struc: 155 a.a.*

Protein chains

O66841  (NUOF_AQUAE) -  NADH-quinone oxidoreductase subunit F from Aquifex aeolicus (strain VF5)

Seq: 426 a.a.

Struc: 416 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.7.1.1.- - ?????

DOI no: 10.1038/s41467-019-10429-0

Nat Commun 10:2551 (2019)

PubMed id: 31186428

A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I.

M.Schulte, K.Frick, E.Gnandt, S.Jurkovic, S.Burschel, R.Labatzke, K.Aierstock, D.Fiegen, D.Wohlwend, S.Gerhardt, O.Einsle, T.Friedrich.

ABSTRACT

Respiratory complex I plays a central role in cellular energy metabolism coupling NADH oxidation to proton translocation. In humans its dysfunction is associated with degenerative diseases. Here we report the structure of the electron input part of Aquifex aeolicus complex I at up to 1.8 Å resolution with bound substrates in the reduced and oxidized states. The redox states differ by the flip of a peptide bond close to the NADH binding site. The orientation of this peptide bond is determined by the reduction state of the nearby [Fe-S] cluster N1a. Fixation of the peptide bond by site-directed mutagenesis led to an inactivation of electron transfer and a decreased reactive oxygen species (ROS) production. We suggest the redox-gated peptide flip to represent a previously unrecognized molecular switch synchronizing NADH oxidation in response to the redox state of the complex as part of an intramolecular feed-back mechanism to prevent ROS production.