Structure of the intact transactivation domain of the human papillomavirus E2 protein
Article Abstract:
It has been possible to identify the crystal structure of the complete human papillomavirus 16 200 amino-acid amino-terminal (E2NT) module refined with data extending to 1.9 angstrom spacing. Two domains, N1 and N2, are arranged to give the module an overall L-shaped appearance. It has been shown that the dimerization of E2NT modules may connect E2 dimers and may function as the key to the formation of DNA loops. It is possible that dimer formation may act as a molecular switch between early gene expression and viral genome replications during human papillomavirus infection.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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Three-dimensional structure of system I of photosynthesis at 6 A resolution
Article Abstract:
Photosystem I (PS I) of the cyanobacterium Synechococcus was mapped out in three dimensions at the six angstrom level using X-ray analysis. PS I contains the reaction centers for photosynthesis, the process by which the higher plants and cyanobacteria derive chemical energy from light energy. PS I is made up of iron-sulphur clusters, chlorophyll a and two large subunits of nine alpha-helices associated through a two-fold rotation axis.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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The structure of trp RNA-binding attenuation protein
Article Abstract:
The trp RNA attenuation protein of Bacillus subtilis' innovative crystal structure, resolved at 1.8 angstrom resolution, has a beta-wheel with a large central hole around which eleven subunits are made stable through eleven intersubunit beta-subunits. Conformational changes are probably induced in flexible residues 25-33 and 49-52 through the L-tryptophan binding in the beta-wheel clefts between adjacent beta-sheets.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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