4rwm

Kuenenia stuttgartiensis hydroxylamine oxidoreductase cryoprotected with ethylene glycol

spinqualitylabelsall models 4rwm, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rwm is a 1 chain structure with sequence from Candidatus kuenenia stuttgartiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, HEC, HEM, HG1, PO4 Related: 4n4j Activity: Hydroxylamine dehydrogenase, with EC number 1.7.2.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Hydroxylamine oxidoreductases (HAOs) contain a unique haem cofactor called P460 that consists of a profoundly ruffled c-type haem with two covalent bonds between the haem porphyrin and a conserved tyrosine. This cofactor is exceptional in that it abstracts electrons from a ligand bound to the haem iron, whereas other haems involved in redox chemistry usually inject electrons into their ligands. The effects of the tyrosine cross-links and of the haem ruffling on the chemistry of this cofactor have been investigated theoretically but are not yet clear. A new crystal structure of an HAO from Candidatus Kuenenia stuttgartiensis, a model organism for anaerobic ammonium oxidation, now shows that its P460 cofactor has yet another unexpected reactivity: when ethylene glycol was used as a cryoprotectant, the 1.8 A resolution electron-density maps showed additional density which could be interpreted as an ethylene glycol molecule covalently bound to the C16 atom of the haem ring, opposite the covalent links to the conserved tyrosine. Possible causes for this unexpected reactivity are discussed. An unexpected reactivity of the P460 cofactor in hydroxylamine oxidoreductase.,Dietl A, Maalcke W, Barends TR Acta Crystallogr D Biol Crystallogr. 2015 Aug;71(Pt 8):1708-13. doi:, 10.1107/S1399004715010706. Epub 2015 Jul 31. PMID:26249351 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA