2o0k
From Proteopedia
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'''T4 gp17 ATPase domain mutant''' | '''T4 gp17 ATPase domain mutant''' | ||
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| + | ==Overview== | ||
| + | Packaging the viral genome into empty procapsids, an essential event in the life cycle of tailed bacteriophages and some eukaryotic viruses, is a process that shares features with chromosome assembly. Most viral procapsids possess a special vertex containing a dodecameric portal protein that is used for entry and exit of the viral genome. The portal and an ATPase are parts of the genome-packaging machine. The ATPase is required to provide energy for translocation and compaction of the negative charges on the genomic DNA. Here we report the atomic structure of the ATPase component in a phage DNA-packaging machine. The bacteriophage T4 ATPase has the greatest similarity to monomeric helicases, suggesting that the genome is translocated by an inchworm mechanism. The similarity of the packaging machines in the double-stranded DNA (dsDNA) bacteriophage T4 and dsRNA bacteriophage varphi12 is consistent with the evolution of many virions from a common ancestor. | ||
==About this Structure== | ==About this Structure== | ||
2O0K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O0K OCA]. | 2O0K is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O0K OCA]. | ||
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| + | ==Reference== | ||
| + | The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids., Sun S, Kondabagil K, Gentz PM, Rossmann MG, Rao VB, Mol Cell. 2007 Mar 23;25(6):943-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17386269 17386269] | ||
[[Category: Enterobacteria phage t4]] | [[Category: Enterobacteria phage t4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Rossmann, M G.]] | [[Category: Rossmann, M G.]] | ||
[[Category: Sun, S.]] | [[Category: Sun, S.]] | ||
| + | [[Category: Hydrolase]] | ||
[[Category: Nucleotide-binding fold]] | [[Category: Nucleotide-binding fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 5 10:08:24 2008'' |
Revision as of 07:08, 5 June 2008
T4 gp17 ATPase domain mutant
Overview
Packaging the viral genome into empty procapsids, an essential event in the life cycle of tailed bacteriophages and some eukaryotic viruses, is a process that shares features with chromosome assembly. Most viral procapsids possess a special vertex containing a dodecameric portal protein that is used for entry and exit of the viral genome. The portal and an ATPase are parts of the genome-packaging machine. The ATPase is required to provide energy for translocation and compaction of the negative charges on the genomic DNA. Here we report the atomic structure of the ATPase component in a phage DNA-packaging machine. The bacteriophage T4 ATPase has the greatest similarity to monomeric helicases, suggesting that the genome is translocated by an inchworm mechanism. The similarity of the packaging machines in the double-stranded DNA (dsDNA) bacteriophage T4 and dsRNA bacteriophage varphi12 is consistent with the evolution of many virions from a common ancestor.
About this Structure
2O0K is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids., Sun S, Kondabagil K, Gentz PM, Rossmann MG, Rao VB, Mol Cell. 2007 Mar 23;25(6):943-9. PMID:17386269 Page seeded by OCA on Thu Jun 5 10:08:24 2008
