6rko | pdb_00006rko

Cryo-EM structure of the E. coli cytochrome bd-I oxidase at 2.68 A resolution

Loading... Status: waiting for Mol* initialization Structural highlights 6rko is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HDD, HEB, OXY, POV, UQ8 Gene: cydB, cyd-2, b0734, JW0723 (ECOLI), cydA, cyd-1, b0733, JW0722 (ECOLI), ynhF, b4602, JW1649.1 (ECOLI), cydX, ybgT, b4515, JW0724 (ECOLI) Activity: Ubiquinol oxidase (electrogenic, proton-motive force generating), with EC number 7.1.1.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CYDX_ECOLI] Required for correct functioning of cytochrome bd-I oxidase. This protein and AppX may have some functional overlap. [CYDB_ECOLI] A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. [CYDA_ECOLI] A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. Publication Abstract from PubMed Cytochrome bd-type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. They are structurally unrelated to mitochondrial cytochrome c oxidases and are therefore a prime target for the development of antimicrobial drugs. We determined the structure of the Escherichia coli cytochrome bd-I oxidase by single-particle cryo-electron microscopy to a resolution of 2.7 angstroms. Our structure contains a previously unknown accessory subunit CydH, the L-subfamily-specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an oxygen-conducting pathway. Comparison with another cytochrome bd oxidase reveals structural divergence in the family, including rearrangement of high-spin hemes and conformational adaption of a transmembrane helix to generate a distinct oxygen-binding site. Active site rearrangement and structural divergence in prokaryotic respiratory oxidases.,Safarian S, Hahn A, Mills DJ, Radloff M, Eisinger ML, Nikolaev A, Meier-Credo J, Melin F, Miyoshi H, Gennis RB, Sakamoto J, Langer JD, Hellwig P, Kuhlbrandt W, Michel H Science. 2019 Oct 4;366(6461):100-104. doi: 10.1126/science.aay0967. PMID:31604309 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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