6CPD

Crystal structure of PmoD soluble domain from Methylocystis sp. ATCC 49242 (Rockwell)

Summary for 6CPD

• Entry DOI: 10.2210/pdb6cpd/pdb
• Descriptor: PmoD, SULFATE ION, COPPER (I) ION, ... (4 entities in total)
• Functional Keywords: copper, cupredoxin, periplasm, metal binding protein
• Biological source: Methylocystis sp. ATCC 49242
• Total number of polymer chains: 2
• Total formula weight: 29138.78

Authors

Fisher, O.S.,Rosenzweig, A.C. (deposition date: 2018-03-13, release date: 2018-10-31, Last modification date: 2019-12-04)

Primary citation

Fisher, O.S.,Kenney, G.E.,Ross, M.O.,Ro, S.Y.,Lemma, B.E.,Batelu, S.,Thomas, P.M.,Sosnowski, V.C.,DeHart, C.J.,Kelleher, N.L.,Stemmler, T.L.,Hoffman, B.M.,Rosenzweig, A.C.
Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria.
Nat Commun, 9:4276-4276, 2018

PubMed Abstract: Methane-oxidizing microbes catalyze the oxidation of the greenhouse gas methane using the copper-dependent enzyme particulate methane monooxygenase (pMMO). Isolated pMMO exhibits lower activity than whole cells, however, suggesting that additional components may be required. A pMMO homolog, ammonia monooxygenase (AMO), converts ammonia to hydroxylamine in ammonia-oxidizing bacteria (AOB) which produce another potent greenhouse gas, nitrous oxide. Here we show that PmoD, a protein encoded within many pmo operons that is homologous to the AmoD proteins encoded within AOB amo operons, forms a copper center that exhibits the features of a well-defined Cu site using a previously unobserved ligand set derived from a cupredoxin homodimer. PmoD is critical for copper-dependent growth on methane, and genetic analyses strongly support a role directly related to pMMO and AMO. These findings identify a copper-binding protein that may represent a missing link in the function of enzymes critical to the global carbon and nitrogen cycles.

PubMed: 30323281
DOI: 10.1038/s41467-018-06681-5

Experimental method

X-RAY DIFFRACTION (1.903 Å)