7p7o | pdb_00007p7o

X-RAY CRYSTAL STRUCTURE OF SPOROSARCINA PASTEURII UREASE INHIBITED BY THE GOLD(I)-DIPHOSPHINE COMPOUND Au(PEt3)2Cl DETERMINED AT 1.87 ANGSTROMS

spinqualitylabelsall models 7p7o, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7p7o 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 1.87Å Ligands: AUF, CXM, EDO, KCX, NI, O, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function URE3_SPOPA Publication Abstract from PubMed A few gold compounds were recently found to show antimicrobial properties in vitro, holding great promise for the discovery of new drugs to overcome antibiotic resistance. Here, the inhibition of the bacterial virulence factor urease by four Au(I)-compounds, namely Au(PEt(3))Cl, Au(PEt(3))Br, Au(PEt(3))I and [Au(PEt(3))(2)]Cl, obtained from the antiarthritic Au(I)-drug Auranofin and earlier reported to act as antimicrobials, is investigated. The three monophosphino Au(I) complexes showed IC(50) values in the 30-100 nM range, while the diphosphino Au(I) complex, though being less active, still showed a IC(50) value of 7 muM. The structural basis for this inhibition was provided by solving the crystal structures of urease co-crystallized with Au(PEt(3))I and [Au(PEt(3))(2)]Cl: at least two Au(I) ions bind the enzyme in a flap domain involved in the catalysis, thus obliterating enzyme activity. Peculiar changes observed in the two structures reveal implications for the mechanism of soft metal binding and enzyme inactivation. Medicinal Au(I) compounds targeting urease as prospective antimicrobial agents: unveiling the structural basis for enzyme inhibition.,Mazzei L, Massai L, Cianci M, Messori L, Ciurli S Dalton Trans. 2021 Oct 19;50(40):14444-14452. doi: 10.1039/d1dt02488d. PMID:34585201 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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