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Science
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Disponibilidad
| Institución detectada | Período | Navegá | Descargá | Solicitá |
|---|---|---|---|---|
| No detectada | desde mar. 1997 / hasta dic. 2023 | Science Journals |
Información
Tipo de recurso:
revistas
ISSN impreso
0036-8075
ISSN electrónico
1095-9203
Editor responsable
American Association for the Advancement of Science (AAAS)
País de edición
Estados Unidos
Fecha de publicación
1880-
Cobertura temática
Tabla de contenidos
Flexibility in DNA Recombination: Structure of the Lambda Integrase Catalytic Core
Hyock Joo Kwon; Radhakrishna Tirumalai; Arthur Landy; Tom Ellenberger
<jats:p> Lambda integrase is archetypic of site-specific recombinases that catalyze intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr <jats:sup>342</jats:sup> is attached to the 3-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of the integrase catalytic domain reveals a protein fold that is conserved in organisms ranging from archaebacteria to yeast and that suggests a model for interaction with target DNA. The attacking Tyr <jats:sup>342</jats:sup> nucleophile is located on a flexible loop about 20 angstroms from a basic groove that contains all the other catalytically essential residues. This bipartite active site can account for several apparently paradoxical features of integrase family recombinases, including the capacity for both cis and trans cleavage of DNA. </jats:p>
Palabras clave: Multidisciplinary.
Pp. 126-131
A Transmembrane Helix Dimer: Structure and Implications
Kevin R. MacKenzie; James H. Prestegard; Donald M. Engelman
<jats:p>The three-dimensional structure of the dimeric transmembrane domain of glycophorin A (GpA) was determined by solution nuclear magnetic resonance spectroscopy of a 40-residue peptide solubilized in aqueous detergent micelles. The GpA membrane-spanning helices cross at an angle of –40 degrees and form a small but well-packed interface that lacks intermonomer hydrogen bonds. The structure provides an explanation for the previously characterized sequence dependence of GpA dimerization and demonstrates that van der Waals interactions alone can mediate stable and specific associations between transmembrane helices.</jats:p>
Palabras clave: Multidisciplinary.
Pp. 131-133
Products & Materials|
Palabras clave: Multidisciplinary.
Pp. 135-136
Science 's Next Wave: Quality Control: A Rapidly Expanding Career Niche
Nicole Ruediger
Palabras clave: Multidisciplinary.
Pp. 139
This Week in Science
Palabras clave: Multidisciplinary.
Pp. 173-173
Breaking HIV-1 entry into cells
Palabras clave: Multidisciplinary.
Pp. 173a-173
Trapping wet melts
Palabras clave: Multidisciplinary.
Pp. 173c-173
Three are crowded
Palabras clave: Multidisciplinary.
Pp. 173d-173