1 to 10 of 16 literature results

• Sequence-structure relationships in polysaccharide co-polymerase (PCP) proteins.

  Polysaccharides are ubiquitously distributed on the cell surface of bacteria. These polymers are involved in many processes, including immune avoidanc…

  Authors: Renato Morona, Leanne Purins, Ante Tocilj, Allan Matte, Miroslaw Cygler

  Source: Trends in biochemical sciences. 2009 Feb

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• The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site.

  BAK/BAX-mediated mitochondrial outer-membrane permeabilization (MOMP) drives cell death during development and tissue homeostasis from zebrafish to hu…

  Authors: Tudor Moldoveanu, Qian Liu, Ante Tocilj, Mark Watson, Gordon Shore, Kalle Gehring

  Source: Molecular cell. 2006 Dec 8

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• Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein.

  Insect antifreeze proteins (AFP) are much more effective than fish AFPs at depressing solution freezing points by ice-growth inhibition. AFP from the …

  Authors: Y C Liou, A Tocilj, P L Davies, Z Jia

  Source: Nature. 2000 Jul 20

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• Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria.

  Ribosomes, the site of protein synthesis, are a major target for natural and synthetic antibiotics. Detailed knowledge of antibiotic binding sites is …

  Authors: F Schlünzen, R Zarivach, J Harms, A Bashan, A Tocilj, R Albrecht, A Yonath, F Franceschi

  Source: Nature. 2001 Oct 25

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• Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution.

  The small ribosomal subunit performs the decoding of genetic information during translation. The structure of that from Thermus thermophilus shows tha…

  Authors: F Schluenzen, A Tocilj, R Zarivach, J Harms, M Gluehmann, D Janell, A Bashan, H Bartels, I Agmon, F Franceschi,…

  Source: Cell. 2000 Sep 1

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• Bacterial polysaccharide co-polymerases share a common framework for control of polymer length.

  The chain length distribution of complex polysaccharides present on the bacterial surface is determined by polysaccharide co-polymerases (PCPs) anchor…

  Authors: Ante Tocilj, Christine Munger, Ariane Proteau, Renato Morona, Leanne Purins, Eunice Ajamian, John Wagner, Magdalene Papadopoulos, Luisa Van Den Bosch, John L Rubinstein,…

  Source: Nature structural & molecular biology. 2008 Feb

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• Crystal structure of heparinase II from Pedobacter heparinus and its complex with a disaccharide product.

  Heparinase II depolymerizes heparin and heparan sulfate glycosaminoglycans, yielding unsaturated oligosaccharide products through an elimination degra…

  Authors: David Shaya, Ante Tocilj, Yunge Li, James Myette, Ganesh Venkataraman, Ram Sasisekharan, Miroslaw Cygler

  Source: The Journal of biological chemistry. 2006 Jun 2

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• Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli.

  The ammonia-producing arginine succinyltransferase pathway is the major pathway in Escherichia coli and related bacteria for arginine catabolism as a …

  Authors: Ante Tocilj, Joseph D Schrag, Yunge Li, Barbara L Schneider, Larry Reitzer, Allan Matte, Miroslaw Cygler

  Source: The Journal of biological chemistry. 2005 Apr 22

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• Structure of an aryl esterase from Pseudomonas fluorescens.

  The structure of PFE, an aryl esterase from Pseudomonas fluorescens, has been solved to a resolution of 1.8 A by X-ray diffraction and shows a charact…

  Authors: Jeremy D Cheeseman, Ante Tocilj, Seongsoon Park, Joseph D Schrag, Romas J Kazlauskas

  Source: Acta crystallographica. Section D, Biological crystallography. 2004 Jul

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• Crystal structure of a dodecameric FMN-dependent UbiX-like decarboxylase (Pad1) from Escherichia coli O157: H7.

  The crystal structure of the flavoprotein Pad1 from Escherichia coli O157:H7 complexed with the cofactor FMN has been determined by the multiple anoma…

  Authors: Erumbi S Rangarajan, Yunge Li, Pietro Iannuzzi, Ante Tocilj, Li-Wei Hung, Allan Matte, Miroslaw Cygler

  Source: Protein science : a publication of the Protein Society. 2004 Nov

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