Journal: Chemical Science

Article Title: Ammonia monooxygenase: a work in progress

doi: 10.1039/d6sc01048b

Figure Lengend Snippet: (A) The AMO heterotrimer in native membranes of N. europaea ATCC 19718, as resolved to 2.77 Å by cryo-EM. α 3 β 3 γ 3 arrangement of the amoA (red), amoB (blue), and amoC (green) subunits shown from the side (left) and the top (right). PDB: 9CL6. (B) The pMMO heterotrimer in native membranes of Methylocystis sp. Rockwell ATCC 49242, as resolved to 2.48 Å by cryo-EM. α 3 β 3 γ 3 arrangement of the pmoA (red), pmoB (blue), and pmoC (green) subunits shown from the side (left) and the top (right). PDB: 9CL5.

Article Snippet: Sequence comparison by Musiani, Ciurli and coworkers of pmoD from Methylocystis sp. ATCC 49242 (Rockwell) and amoD/E from N. europaea demonstrate 38% and 28% sequence identity, respectively.

Techniques: Cryo-EM Sample Prep

Journal: Chemical Science

Article Title: Ammonia monooxygenase: a work in progress

doi: 10.1039/d6sc01048b

Figure Lengend Snippet: The AMO (A) and pMMO (B) trimer, with the exogenous helix of unknown function along the face of the amoC/pmoC subunit, shown in pink. AMO from PDB: 9CL6, from N. europaea ATCC 19718, as resolved to 2.77 Å by cryo-EM. pMMO from PDB: 9CL5, from Methylocystis sp. ATCC 49242, as resolved to 2.48 Å by cryo-EM.

Article Snippet: Sequence comparison by Musiani, Ciurli and coworkers of pmoD from Methylocystis sp. ATCC 49242 (Rockwell) and amoD/E from N. europaea demonstrate 38% and 28% sequence identity, respectively.

Techniques: Cryo-EM Sample Prep

Journal: Chemical Science

Article Title: Ammonia monooxygenase: a work in progress

doi: 10.1039/d6sc01048b

Figure Lengend Snippet: (A) The His-brace motif from a lytic polysaccharide monooxygenase (LPMO) originating in species Phytophthora infestans T30-4 , as characterized by X-ray diffraction to 1.01 Å. (PDB: 6Z5Y). (B) The Cu B site in pMMO from Methylocystis sp. ATCC 49242, as resolved to 2.48 Å by cryo-EM. (PDB: 9CL5). (C) The Cu B site in AMO from N. europaea ATCC 19718, as resolved to 2.77 Å by cryo-EM. (PDB: 9CL6).

Article Snippet: Sequence comparison by Musiani, Ciurli and coworkers of pmoD from Methylocystis sp. ATCC 49242 (Rockwell) and amoD/E from N. europaea demonstrate 38% and 28% sequence identity, respectively.

Techniques: Cryo-EM Sample Prep

Journal: Chemical Science

Article Title: Ammonia monooxygenase: a work in progress

doi: 10.1039/d6sc01048b

Figure Lengend Snippet: Overlay of the cryo-EM structures containing Cu D site from pmoC ( Methylocystis sp. ATCC 49242, 2.48 Å cryo-EM) (PDB: 9CL5) and a metal-free Cu D site from amoC ( N. europaea ATCC 19718, 2.77 Å cryo-EM) (PDB: 9CL6). pmoC is shown in green, while amoC is shown in cyan. Residues from pmoC are shown in parentheses, while those from amoC are not.

Article Snippet: Sequence comparison by Musiani, Ciurli and coworkers of pmoD from Methylocystis sp. ATCC 49242 (Rockwell) and amoD/E from N. europaea demonstrate 38% and 28% sequence identity, respectively.

Techniques: Cryo-EM Sample Prep

Journal: Chemical Science

Article Title: Ammonia monooxygenase: a work in progress

doi: 10.1039/d6sc01048b

Figure Lengend Snippet: The structure of monomeric pmoD from Methylocystis sp. ATCC 49242, as observed by X-ray diffraction to 1.90 Å resolution (PDB: 6CPD). On the left is the structure of the homodimer, as purified. On the right, the ligands binding to the Cu ion are shown with corresponding distances. Note that this is the monomeric form of the protein, which does not contain the Cu A site formed by the homodimeric species.

Article Snippet: Sequence comparison by Musiani, Ciurli and coworkers of pmoD from Methylocystis sp. ATCC 49242 (Rockwell) and amoD/E from N. europaea demonstrate 38% and 28% sequence identity, respectively.

Techniques: Purification, Binding Assay

Journal: The ISME Journal

Article Title: Verrucomicrobiota are specialist consumers of sulfated methyl pentoses during diatom blooms

doi: 10.1038/s41396-021-01105-7

Figure Lengend Snippet: The maximum-likelihood tree was based on a group of 120 conserved genes. Taxonomic classifications were determined using GTDB-tk. All orders in the external ring (coloured) belong to the Verrucomicrobiae class. Families containing ten or more genomes are highlighted (internal ring). Recovered MAGs from Helgoland are named according to their family affiliation and are highlighted by red circles. Branch support values between 90 and 100% are represented by dots. Names at the branches for isolates are shown in grey. Yellow triangles highlight branches for other isolates related at the genus/species level to those named. Abbreviated name in the second ring corresponds to Verrucomicrobiaceae . Complete names for abbreviated isolates: Coraliomargarita akajimensis DSM 45221, Verrucomicrobia bacterium IMCC26134, Cephaloticoccus capnophilus CV41, Cephaloticoccus primus CAG34, Nibricoccus aquaticus HZ-65, Opitutaceae bacterium EW11, Lacunisphaera limnophila IG16b, Verrucomicrobiae bacterium DG1235, Rubritalea marina DSM 17716, Prosthecobacter debontii ATCC 700200, Verrucomicrobium spinosum DSM 4136, Verrucomicrobium sp. BvORR106, Methylacidiphilum infernorum V4, Verrucomicrobium sp. GAS474, Verrucomicrobia bacterium LW23.

Article Snippet: Complete names for abbreviated isolates: Coraliomargarita akajimensis DSM 45221, Verrucomicrobia bacterium IMCC26134, Cephaloticoccus capnophilus CV41, Cephaloticoccus primus CAG34, Nibricoccus aquaticus HZ-65, Opitutaceae bacterium EW11, Lacunisphaera limnophila IG16b, Verrucomicrobiae bacterium DG1235, Rubritalea marina DSM 17716, Prosthecobacter debontii ATCC 700200, Verrucomicrobium spinosum DSM 4136, Verrucomicrobium sp. BvORR106, Methylacidiphilum infernorum V4, Verrucomicrobium sp. GAS474, Verrucomicrobia bacterium LW23.

Techniques: