6yl3

High resolution cryo-EM structure of urease from the pathogen Yersinia enterocoliticaHigh resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica

Structural highlights 6yl3 is a 36 chain structure with sequence from Yersinia enterocolitica w22703. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NonStd Res: Activity: Urease, with EC number 3.5.1.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Urease converts urea into ammonia and carbon dioxide and makes urea available as a nitrogen source for all forms of life except animals. In human bacterial pathogens, ureases also aid in the invasion of acidic environments such as the stomach by raising the surrounding pH. Here, we report the structure of urease from the pathogen Yersinia enterocolitica at 2 A resolution from cryo-electron microscopy. Y. enterocolitica urease is a dodecameric assembly of a trimer of three protein chains, ureA, ureB and ureC. The high data quality enables detailed visualization of the urease bimetal active site and of the impact of radiation damage. The obtained structure is of sufficient quality to support drug development efforts. High-resolution cryo-EM structure of urease from the pathogen Yersinia enterocolitica.,Righetto RD, Anton L, Adaixo R, Jakob RP, Zivanov J, Mahi MA, Ringler P, Schwede T, Maier T, Stahlberg H Nat Commun. 2020 Oct 9;11(1):5101. doi: 10.1038/s41467-020-18870-2. PMID:33037208 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6yl3, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image