Structure of a viral procapsid with molecular scaffolding
Article Abstract:
Researchers demonstrate the function of scaffolding proteins in the assembly of a macromolecular structure. Knowledge of macromolecular assembly is particularly relevant to the study of viral systems. The researchers present the structure of a procapsid-like particle at 3.5-A resolution and illustrate how the scaffolding proteins B and D coordinate assembly of the virus through their interactions with F and G proteins. The presence of B and D proteins enables preformed pentamers to form into a shell by means of contact across the icosahedral 2-fold axes. This then allows closing of the 3-fold holes to consolidate the virion assembly.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Crystal structure of the met repressor-operator complex at 2.8A resolution reveals DNA recognition by beta-strands
Article Abstract:
Gene regulation by proteins that attach to specific sequences in DNA is made possible by the met repressor-operator complex's crystal structure. This structure, observable at 2.8 angstrom resolution, consists of two dimeric repressor molecules linked to adjacent sites separated by eight base pairs on an 18-base-pair DNA fragment. Insertion of double-stranded antiparallel protein beta-ribbons or strands effects the selection of particular DNA sequences.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1992
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Structure of the bacteriophage phi29 DNA packaging motor
Article Abstract:
The DNA packaging mechanism of the bacillus subtilis bacteriophage phi29 is described.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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