Summary for 9FEK
| Entry DOI | 10.2210/pdb9fek/pdb |
| Descriptor | Putative agmatinase 2, SULFATE ION, MANGANESE (II) ION, ... (5 entities in total) |
| Functional Keywords | comammox, guanidine, guanidinase, complete ammonia oxidizer, metal binding protein |
| Biological source | Candidatus Nitrospira inopinata |
| Total number of polymer chains | 12 |
| Total formula weight | 504266.57 |
| Authors | Puehringer, D.,Mccarthy, A. (deposition date: 2024-05-20, release date: 2024-08-14, Last modification date: 2024-10-02) |
| Primary citation | Palatinszky, M.,Herbold, C.W.,Sedlacek, C.J.,Puhringer, D.,Kitzinger, K.,Giguere, A.T.,Wasmund, K.,Nielsen, P.H.,Dueholm, M.K.D.,Jehmlich, N.,Gruseck, R.,Legin, A.,Kostan, J.,Krasnici, N.,Schreiner, C.,Palmetzhofer, J.,Hofmann, T.,Zumstein, M.,Djinovic-Carugo, K.,Daims, H.,Wagner, M. Growth of complete ammonia oxidizers on guanidine. Nature, 633:646-653, 2024 Cited by PubMed Abstract: Guanidine is a chemically stable nitrogen compound that is excreted in human urine and is widely used in manufacturing of plastics, as a flame retardant and as a component of propellants, and is well known as a protein denaturant in biochemistry. Guanidine occurs widely in nature and is used by several microorganisms as a nitrogen source, but microorganisms growing on guanidine as the only substrate have not yet been identified. Here we show that the complete ammonia oxidizer (comammox) Nitrospira inopinata and probably most other comammox microorganisms can grow on guanidine as the sole source of energy, reductant and nitrogen. Proteomics, enzyme kinetics and the crystal structure of a N. inopinata guanidinase homologue demonstrated that it is a bona fide guanidinase. Incubation experiments with comammox-containing agricultural soil and wastewater treatment plant microbiomes suggested that guanidine serves as substrate for nitrification in the environment. The identification of guanidine as a growth substrate for comammox shows an unexpected niche of these globally important nitrifiers and offers opportunities for their isolation. PubMed: 39143220DOI: 10.1038/s41586-024-07832-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.58 Å) |
Structure validation
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