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Structural basis for the nuclease activity of a bacteriophage large terminase

Structural basis for the nuclease activity of a bacteriophage large terminase

http://www.wikidata.org/entity/Q27655480

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Clamp loader ATPases and the evolution of DNA replication machinery.Structure and inhibition of herpesvirus DNA packaging terminase nuclease domain Small Terminase Couples Viral DNA Binding to Genome-Packaging ATPase Activity Crystal structure of the primary piRNA biogenesis factor Zucchini reveals similarity to the bacterial PLD endonuclease Nuc Structural basis for DNA recognition and loading into a viral packaging motor The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding The Structure of the Herpes Simplex Virus DNA-Packaging Terminase pUL15 Nuclease Domain Suggests an Evolutionary Lineage among Eukaryotic and Prokaryotic Viruses Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage Large Terminase Conformational Change Induced by Connector Binding in Bacteriophage T7 Structure of P22 Headful Packaging Nuclease Mechanisms of DNA Packaging by Large Double-Stranded DNA Viruses Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain.The large terminase DNA packaging motor grips DNA with its ATPase domain for cleavage by the flexible nuclease domain.Specificity of interactions among the DNA-packaging machine components of T4-related bacteriophages.Regulation by interdomain communication of a headful packaging nuclease from bacteriophage T4.Automated classification of tailed bacteriophages according to their neck organization.Designing a nine cysteine-less DNA packaging motor from bacteriophage T4 reveals new insights into ATPase structure and function.Architecture of the Complex Formed by Large and Small Terminase Subunits from Bacteriophage P22.Two distinct modes of metal ion binding in the nuclease active site of a viral DNA-packaging terminase: insight into the two-metal-ion catalytic mechanism.The enzymology of a viral genome packaging motor is influenced by the assembly state of the motor subunits.The nuclease domain of the SPP1 packaging motor coordinates DNA cleavage and encapsidation.Divergent Evolution of Nuclear Localization Signal Sequences in Herpesvirus Terminase Subunits.The C-terminal domain of the bacteriophage T4 terminase docks on the prohead portal clip region during DNA packaging.Staphylococcal pathogenicity island DNA packaging system involving cos-site packaging and phage-encoded HNH endonucleases.The DNA-packaging nanomotor of tailed bacteriophages.Viral genome packaging terminase cleaves DNA using the canonical RuvC-like two-metal catalysis mechanism.Direct interaction of the bacteriophage SPP1 packaging ATPase with the portal protein.Molecular architecture of tailed double-stranded DNA phages.Structure of the large terminase from a hyperthermophilic virus reveals a unique mechanism for oligomerization and ATP hydrolysis.Breaking Symmetry in Viral Icosahedral Capsids as Seen through the Lenses of X-ray Crystallography and Cryo-Electron Microscopy.

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P2860

Structural basis for the nuclease activity of a bacteriophage large terminase

http://www.wikidata.org/entity/Q27655480

description

2009 nî lūn-bûn

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2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2009 թվականի հունիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Structural basis for the nuclease activity of a bacteriophage large terminase

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Structural basis for the nuclease activity of a bacteriophage large terminase

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Structural basis for the nuclease activity of a bacteriophage large terminase

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Structural basis for the nuclease activity of a bacteriophage large terminase

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Structural basis for the nuclease activity of a bacteriophage large terminase

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Structural basis for the nuclease activity of a bacteriophage large terminase

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Structural basis for the nuclease activity of a bacteriophage large terminase

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Structural basis for the nuclease activity of a bacteriophage large terminase

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Structural basis for the nuclease activity of a bacteriophage large terminase

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Structural basis for the nuclease activity of a bacteriophage large terminase

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Andrew W Foster

http://www.w3.org/2001/XMLSchema#string

Maria Chechik

http://www.w3.org/2001/XMLSchema#string

Mikhail B Shevtsov

http://www.w3.org/2001/XMLSchema#string

Oleg V Kovalevskiy

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P2860

A general two-metal-ion mechanism for catalytic RNA

Structure of human RNase H1 complexed with an RNA/DNA hybrid: insight into HIV reverse transcription

The structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces

Crystal structure of globular domain of histone H5 and its implications for nucleosome binding

Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions

Making and breaking nucleic acids: two-Mg2+-ion catalysis and substrate specificity

ElNemo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement

Genetic evidence that recognition of cosQ, the signal for termination of phage lambda DNA packaging, depends on the extent of head filling

The terminase enzyme from bacteriophage lambda: a DNA-packaging machine.

The functional domains of bacteriophage t4 terminase.

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592-8

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10.1038/EMBOR.2009.53

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