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1.
Kondo J Pachamuthu K François B Szychowski J Hanessian S Westhof E 《ChemMedChem》2007,2(11):1631-1638
The crystal structure of the complex between oligonucleotide containing the bacterial ribosomal decoding site (A site) and the synthetic paromomycin analogue 1, which contains the gamma-amino-alpha-hydroxybutyryl (L-haba) group at position N1 of ring II (2-DOS ring), and an ether chain with an O-phenethylaminoethyl group at position C2' of ring III, is reported. Interestingly, next to the paromomycin analogue 1 specifically bound to the A site, a second molecule of 1 with a different conformation is observed at the crystal packing interface which mimics the A-minor interaction between two bulged-out adenines from the A site and the codon-anticodon stem of the mRNA-tRNA complex. Improved antibacterial activity supports the conclusion that analogue 1 might affect protein synthesis on the ribosome in two different ways: 1) specific binding to the A site forces maintenance of the "on" state with two bulged out adenines, and 2) a new binding mode of 1 to an A-minor motif which stabilizes complex formation between the ribosome and the mRNA-tRNA complex regardless of whether the codon-anticodon stem is of the cognate or near-cognate type. 相似文献
2.
Wilmanns Matthias; Schlagenhauf Edith; Fol Bruno; Jansonius Johan N 《Protein engineering, design & selection : PEDS》1990,3(3):173-180
The recombinant synthase domain of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilateisomerase:indole-3-glycerol-phosphate synthase from Escherichiacoli has been crystallized, and the structure has been solvedat 4 Å resolution. Two closely related crystal forms grownfrom ammonium sulphate diffract to 2 Å resolution. Oneform (space group R32, a = 163 Å, = 29.5°) containsthe unliganded synthase domain; the second crystal form (spacegroup P6322, a = 144 Å, c = 158 Å) is co-crystallizedwith the substrate analogue N-(5'-phosphoribit-1-yl)anthranilate.The structure of the synthaseinhibitor complex has beensolved by the molecular replacement method. This achievementrepresents the first successful use of a (ß)g-barrelmonomer as a trial model. The recombinant synthase domain associatesas a trimer in the crystal, the molecules being related by apseudo-crystallographic triad. The interface contacts betweenthe three domains are mediated by those residues that are alsoinvolved in the domain interface of the bifunctional enzyme.This system provides a model for an interface which is usedin both intermolecular and intramolecular domain contacts. 相似文献
3.
Pavel Gentschev Matthias Lüken Niclas Mller Annette Rompel Bernt Krebs 《Inorganic chemistry communications》2001,4(12):3838
Reaction of the ligand N,N,N′,N′-bis[(2-hydroxybenzyl)(N-methylimidazolyl)]-2-ol-1,3-propendiamine (Hbhbmipo) with copper(II) perchlorate and sodium acetate in acetonitrile/ethanol leads to the assembly of a novel dinuclear copper(II) complex. The crystal structure, magnetic properties and its catecholase activity are reported. Both copper(II) ions are set in a distorted square pyramidal coordination sphere with a N2O3 donor set resulting in a CuCu distance of 3.382(5) Å. To our knowledge this is the first example of a dinuclear Cu(II) complex with square pyramidal coordination geometry in which the N2O3 donor set contains N-imidazol and O-phenol. The complex represents a structural model for a tyrosine intermediate in the proposed mechanism during hydroxylation of monophenols. 相似文献