| 1. |
- Golmohammadi, R, et al.
(författare)
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The crystal structure of bacteriophage Q beta at 3.5 angstrom resolution
- 1996
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Ingår i: STRUCTURE. - : CURRENT BIOLOGY LTD. - 0969-2126. ; 4:5, s. 543-554
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- Background: The capsid protein subunits of small RNA bacteriophages form a T=3 particle upon assembly and RNA encapsidation. Dimers of the capsid protein repress translation of the replicase gene product by binding to the ribosome binding site and this in
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| 2. |
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| 3. |
- Lloyd, MD, et al.
(författare)
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Studies on the active site of deacetoxycephalosporin C synthase
- 1999
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Ingår i: JOURNAL OF MOLECULAR BIOLOGY. - : ACADEMIC PRESS LTD. - 0022-2836. ; 287:5, s. 943-960
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Tidskriftsartikel (refereegranskat)abstract
- The Fe(II) and 2-oxogolutarate-dependent dioxygenase deacetoxycephalosporin C synthase (DAOCS) from Streptomyces clavuligerus was expressed at ca 25% of total soluble protein in Escherichia coli and purified by an efficient large-scale procedure. Purified
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| 4. |
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| 5. |
- van, den Worm SHE, et al.
(författare)
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Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments
- 1998
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Ingår i: NUCLEIC ACIDS RESEARCH. - : OXFORD UNIV PRESS. - 0305-1048. ; 26:5, s. 1345-1351
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- In MS2 assembly of phage particles results from an interaction between a coat protein dimer and a stem-loop of the RNA genome (the operator hairpin), Amino acid residues Thr45, which is universally conserved among the small RNA phages, and Thr59 are part
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| 6. |
- Gunn, Laura, 1986-, et al.
(författare)
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A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphatecarboxylase/oxygenase (Rubisco) acts as a small subunit mimic
- 2017
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Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 292:16, s. 6838-6850
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Tidskriftsartikel (refereegranskat)abstract
- The catalytic inefficiencies of the CO2-fixing enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) often limit plant productivity. Strategies to engineer more efficient plant Rubiscos have been hampered by evolutionary constraints, prompting interest in Rubisco isoforms from non-photosynthetic organisms. The methanogenic archaeon Methanococcoides burtonii contains a Rubisco isoform that functions to scavenge the ribulose-1,5-bisphosphate (RuBP) byproduct of purine/pyrimidine metabolism. The crystal structure of M. burtonii Rubisco (MbR) presented here at 2.6 Å resolution is composed of catalytic large subunits (LSu) assembled into pentamers of dimers, (L2)5 and differs from Rubiscos from higher plants where LSus are glued together by small subunits (SSu) into hexadecameric L8S8 enzymes. MbR contains a unique 29-amino-acid insertion near the C-terminus, which folds as a separate domain in the structure. This domain, which is visualized for the first time in this study, is located in a similar position to SSus in L8S8 enzymes between LSus of adjacent L2 dimers, where negatively charged residues co-ordinate around a Mg2+ ion in a fashion that suggests this domain may be important for the assembly process. The Rubisco assembly domain is thus an inbuilt SSu mimic that concentrates L2 dimers. MbR assembly is ligand-stimulated and we show that only 6-carbon molecules with a particular stereochemistry at the C3 carbon can induce oligomerization. Based on MbR structure, subunit arrangement, sequence, phylogenetic distribution and function, MbR and a subset of Rubiscos from the Methanosarcinales order are proposed to belong to a new Rubisco sub-group, named form IIIB.
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| 7. |
- STOCKLEY, PG, et al.
(författare)
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MOLECULAR MECHANISM OF RNA PHAGE MORPHOGENESIS
- 1994
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Ingår i: INTERNATIONAL JOURNAL OF BIOCHEMISTRY. - : PERGAMON-ELSEVIER SCIENCE LTD. ; 26:10-11, s. 1249-1260
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Recension (övrigt vetenskapligt/konstnärligt)abstract
- Recent progress on the molecular mechanism of RNA phage morphogenesis is described. Functional studies, both in vivo and in vitro, are correlated with the latest structural studies on phages, their capsids and the assembly initiation RNA stem-loop.
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| 8. |
- STOCKLEY, PG, et al.
(författare)
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PROBING SEQUENCE-SPECIFIC RNA RECOGNITION BY THE BACTERIOPHAGE-MS2 COAT PROTEIN
- 1995
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Ingår i: NUCLEIC ACIDS RESEARCH. - : OXFORD UNIV PRESS UNITED KINGDOM. - 0305-1048. ; 23:13, s. 2512-2518
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- We present the results of in vitro binding studies aimed at defining the key recognition elements on the MS2 RNA translational operator (TR) essential for complex formation with coat protein. We have used chemically synthesized operators carrying modified
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| 9. |
- Stonehouse, NJ, et al.
(författare)
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Crystal structures of MS2 capsids with mutations in the subunit FG loop
- 1996
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Ingår i: JOURNAL OF MOLECULAR BIOLOGY. - : ACADEMIC PRESS LTD. - 0022-2836. ; 256:2, s. 330-339
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- The loop between the F and G beta strands (FG loop) of the bacteriophage MS2 coat protein subunit forms inter-subunit contacts around the 5-fold and 3-fold (quasi 6-fold) axes of the T = 3 protein shell. In capsids, the loop is found in two very different
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| 10. |
- Valegard, K, et al.
(författare)
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Structure of a cephalosporin synthase
- 1998
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Ingår i: NATURE. - : MACMILLAN MAGAZINES LTD. - 0028-0836. ; 394:6695, s. 805-809
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Tidskriftsartikel (refereegranskat)abstract
- Penicillins and cephalosporins are among the most widely used therapeutic agents. These antibiotics are produced from fermentation-derived materials as their chemical synthesis is not commercially viable. Unconventional steps in their biosynthesis are cat
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| 11. |
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