6qdy | pdb_00006qdy

The crystal structure of Sporosarcina pasteurii urease in complex with its substrate urea

spinqualitylabelsall models 6qdy, resolution 1.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qdy is a 3 chain structure with sequence from Sporosarcina pasteurii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.416Å Ligands: CXM, EDO, F, KCX, NI, SO4, URE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function URE3_SPOPA Publication Abstract from PubMed Urease, the most efficient enzyme known, contains an essential dinuclear Ni(II) cluster in the active site. It catalyzes the hydrolysis of urea, inducing a rapid pH increase that has negative effects on human health and agriculture. Thus, the control of urease activity is of utmost importance in medical, pharmaceutical, and agro-environmental applications. All known urease inhibitors are either toxic or inefficient. The development of new and efficient chemicals able to inhibit urease relies on the knowledge of all steps of the catalytic mechanism. The short (microseconds) lifetime of the urease-urea complex has hampered the determination of its structure. The present study uses fluoride to substitute the hydroxide acting as the co-substrate in the reaction, preventing the occurrence of the catalytic steps that follow substrate binding. The 1.42 A crystal structure of the urease-urea complex, reported here, resolves the enduring debate on the mechanism of this metalloenzyme. The Structure of the Elusive Urease-Urea Complex Unveils the Mechanism of a Paradigmatic Nickel-Dependent Enzyme.,Mazzei L, Cianci M, Benini S, Ciurli S Angew Chem Int Ed Engl. 2019 May 27;58(22):7415-7419. doi:, 10.1002/anie.201903565. Epub 2019 Apr 30. PMID:30969470 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Urease 3D structures

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