P15 and P3, the Tail Completion Proteins of Bacteriophage T4, Both Form Hexameric Rings

Li, Zhao; Kanamaru, Shuji; Chaidirek, Chatree'chalerm; Arisaka, Fumio

doi:10.1128/jb.185.5.1693-1700.2003

Cited by 21 publications

(21 citation statements)

References 24 publications

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“…Analytical ultracentrifugation was performed as described (Zhao et al., 2003), and frictional coefficients were determined using f ∝ M/S for each species (f, frictional coefficient; M, molecular weight; S, sedimentation coefficient).…”

Section: Methodsmentioning

confidence: 99%

AAA+ Ring and Linker Swing Mechanism in the Dynein Motor

Roberts

Numata

Walker³

et al. 2009

Cell

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207

229

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SummaryDynein ATPases power diverse microtubule-based motilities. Each dynein motor domain comprises a ring-like head containing six AAA+ modules and N- and C-terminal regions, together with a stalk that binds microtubules. How these subdomains are arranged and generate force remains poorly understood. Here, using electron microscopy and image processing of tagged and truncated Dictyostelium cytoplasmic dynein constructs, we show that the heart of the motor is a hexameric ring of AAA+ modules, with the stalk emerging opposite the primary ATPase site (AAA1). The C-terminal region is not an integral part of the ring but spans between AAA6 and near the stalk base. The N-terminal region includes a lever-like linker whose N terminus swings by ∼17 nm during the ATPase cycle between AAA2 and the stalk base. Together with evidence of stalk tilting, which may communicate changes in microtubule binding affinity, these findings suggest a model for dynein's structure and mechanism.

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Section: Methodsmentioning

confidence: 99%

AAA+ Ring and Linker Swing Mechanism in the Dynein Motor

Roberts

Numata

Walker³

et al. 2009

Cell

Self Cite

207

229

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“…In the absence of the tail tube, gp18 assembles into long polysheaths with a structure similar in several aspects to the contracted state [64,65]. Both the tail tube and the tail sheath have helical symmetry with a pitch of 40.6 Å and successive subunits repeated every 17.7° [66,67]. Assembled tail sheath represents a metastable supramolecular structure, and sheath contraction is an irreversible process.…”

Section: Tail Structurementioning

confidence: 97%

Molecular architecture of bacteriophage T4

Mesyanzhinov

Leiman

Kostyuchenko

et al. 2004

Biochemistry (Moscow)

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In studying bacteriophage T4--one of the basic models of molecular biology for several decades--there has come a Renaissance, and this virus is now actively used as object of structural biology. The structures of six proteins of the phage particle have recently been determined at atomic resolution by X-ray crystallography. Three-dimensional reconstruction of the infection device--one of the most complex multiprotein components--has been developed on the basis of cryo-electron microscopy images. The further study of bacteriophage T4 structure will allow a better understanding of the regulation of protein folding, assembly of biological structures, and also mechanisms of functioning of the complex biological molecular machines.

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“…The length of the tail sheath is determined by the length of the tube. The assembly of the tail is completed by attachment of a gp15 hexamer to the last ring of the tail sheath [87]. CryoEM reconstruction of the baseplate-tail tube complex [80] shows that the baseplate is a dome-shaped object which is 270 Å high and 520 Å in diameter at its widest part ( fig.…”

Section: The Tail Fibers and Infection Processmentioning

confidence: 99%

Structure and morphogenesis of bacteriophage T4

Leiman

Kanamaru

Mesyanzhinov³

et al. 2003

Cellular and Molecular Life Sciences (CMLS)

237

217

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Bacteriophage T4 is one of the most complex viruses. More than 40 different proteins form the mature virion, which consists of a protein shell encapsidating a 172-kbp double-stranded genomic DNA, a 'tail,' and fibers, attached to the distal end of the tail. The fibers and the tail carry the host cell recognition sensors and are required for attachment of the phage to the cell surface. The tail also serves as a channel for delivery of the phage DNA from the head into the host cell cytoplasm. The tail is attached to the unique 'portal' vertex of the head through which the phage DNA is packaged during head assembly. Similar to other phages, and also herpes viruses, the unique vertex is occupied by a dodecameric portal protein, which is involved in DNA packaging.

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P15 and P3, the Tail Completion Proteins of Bacteriophage T4, Both Form Hexameric Rings

Cited by 21 publications

References 24 publications

AAA+ Ring and Linker Swing Mechanism in the Dynein Motor

AAA+ Ring and Linker Swing Mechanism in the Dynein Motor

Molecular architecture of bacteriophage T4

Structure and morphogenesis of bacteriophage T4

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