Structure of P22 Headful Packaging Nuclease

Roy, Ankoor; Cingolani, Gino

doi:10.1074/jbc.m112.349894

Cited by 54 publications

(87 citation statements)

References 51 publications

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“…48,49 In addition crystal structures the large terminase nuclease domains of the phages SPP1, P22, and a T4-like phage RB69 are available. 48,50,51 The N-terminal ATPase domains of large terminases have a classical oligonucleotide-binding fold, 52 whereas their C-terminal nuclease domains have a ribonuclease H-like fold. Based on the studies of the T4 large (gp17, 70 kDa) and small (gp16, 18 kDa) terminases, and the cryo-EM reconstruction of the T4 capsid complexed with the large terminase, a model for the packaging initiation and DNA translocation was proposed (Figs.…”

Section: Capsid Assemblymentioning

confidence: 99%

Molecular architecture of tailed double-stranded DNA phages

2014

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Section: Capsid Assemblymentioning

confidence: 99%

Molecular architecture of tailed double-stranded DNA phages

2014

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“…Terminases contain a nuclease domain that is responsible for cleavage of viral DNA concatemer into genomelength units. Despite low sequence identity (<15%), the gp2 C-terminal domain exhibits a fold that not only is homologous to viral terminase nuclease domain structures (13,14,18,19), but also clearly resembles those of a large group of nucleases such as RNases H, topoisomerases, integrases, and DNA/RNA polymerases, which use similar metal-ion catalytic mechanisms (30,31). (Fig.…”

Section: Viral Dna-packaging Motors May Represent a Unique Clade Of Nmentioning

confidence: 99%

“…Positively charged residues K192, R193, and R200 from the linker domain also make contact with the DNA phosphate backbone. Preceding the helix α16 is a hairpin structure that is conserved among viral terminase nuclease domains, and such structural elements in phages SPP1 and P22 were proposed to mediate interaction with DNA (14,18). In our model, that hairpin is also involved in interaction with the docked DNA through residue K416.…”

Section: Nuclease Domain and Linker Domain Together Form The Dna-bindingmentioning

confidence: 99%

Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage

Zhao

Christensen

Kamau

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

102

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Many DNA viruses use powerful molecular motors to cleave concatemeric viral DNA into genome-length units and package them into preformed procapsid powered by ATP hydrolysis. Here we report the structures of the DNA-packaging motor gp2 of bacteriophage Sf6, which reveal a unique clade of RecA-like ATPase domain and an RNase H-like nuclease domain tethered by a regulatory linker domain, exhibiting a strikingly distinct domain arrangement. The gp2 structures complexed with nucleotides reveal, at the atomic detail, the catalytic center embraced by the ATPase domain and the linker domain. The gp2 nuclease activity is modulated by the ATPase domain and is stimulated by ATP. An extended DNA-binding surface is formed by the linker domain and the nuclease domain. These results suggest a unique mechanism for translation of chemical reaction into physical motion of DNA and provide insights into coordination of DNA translocation and cleavage in a viral DNA-packaging motor, which may be achieved via linker-domain-mediated interdomain communication driven by ATP hydrolysis.terminase | virus assembly | genome packaging M ost double-stranded DNA (dsDNA) viruses package their genome into preformed protein shells in an active manner using virally encoded molecular motors, as in tailed dsDNA bacteriophages (1, 2), herpesviruses (3), adenoviruses (4), and poxviruses (5). In tailed dsDNA bacteriophages and herpesviruses, the newly synthesized viral DNA in host cells exists as tandem concatemers, each composed of multiple copies of unit-length genome (6, 7). The viral DNA-packaging motor (also known as terminase large subunit or large terminase) cleaves concatemeric viral DNA into units of or near the genomic length and pumps each into a preformed capsid precursor termed procapsid powered by ATP hydrolysis (2,6,8).The DNA-packaging motors of dsDNA bacteriophages package DNA highly densely into the capsid, resulting in an internal pressure of as high as 50 atmospheres, more than 10 times that found in any other living system (9, 10). These molecular motors can work against a force larger than 50 pN and package DNA at high rates, placing them among the most powerful molecular motors in nature (9, 11). Most phage DNA packaging motor proteins are bifunctional enzymes that integrate two types of enzymatic activities, the ATPase and the nuclease, as required by the concatemeric nature of the packaging substrates. Resolving DNA concatemers into units and packaging into procapsid must be precisely coordinated, and the nuclease activity may only be activated at the initiation step of DNA packaging and upon completion of each packaging cycle.Structures of phage T4 terminase large subunit gp17 revealed an ATPase domain belonging to the additional-strand catalytic glutamate (ASCE) superfamily, and a model for DNA translocation dependent on electrostatic forces was proposed (12, 13). Nevertheless, this model was not supported by the structure of phage SPP1 G2P nuclease domain, as the proposed secondary DNA-binding surface during DNA translocation...

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“…To date the crystal structures of a few terminases have been determined, but none of them are in a complex with DNA ( de Beer et al, 2002;Zhao et al, 2010;Roy & Cingolani, 2012). The recent determination of the 4 Å resolution crystal structure of full-length SF6 G1P has allowed the proposal of a DNA-binding model characterized by the DNA wrapping around the outside of a nine-subunit G1P oligomer as in the nucleosome (Bü ttner et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding

Benini

Chechik

Lombardia

et al. 2013

Acta Crystallogr F Struct Biol Cryst Commun

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PDB Reference: DNA-binding domain of the bacteriophage SF6 small terminase subunit, 2cmp DNA packaging in tailed bacteriophages and in evolutionarily related herpesviruses is controlled by a viral-encoded terminase. As in a number of other phages, in the Bacillus subtilis bacteriophages SF6 and SPP1 the terminase complex consists of two proteins: G1P and G2P. The crystal structure of the N-terminal DNA-binding domain of the bacteriophage SF6 small terminase subunit G1P is reported. Structural comparison with other DNA-binding proteins allows a general model for the interaction of G1P with the packaginginitiation site to be proposed.

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Structure of P22 Headful Packaging Nuclease

Cited by 54 publications

References 51 publications

Molecular architecture of tailed double-stranded DNA phages

Molecular architecture of tailed double-stranded DNA phages

Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage

The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on DNA binding

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