1fou: Difference between revisions

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New page: left|200px<br /><applet load="1fou" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fou, resolution 3.2Å" /> '''CONNECTOR PROTEIN FRO...
 
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[[Image:1fou.gif|left|200px]]<br /><applet load="1fou" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fou.gif|left|200px]]<br /><applet load="1fou" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fou, resolution 3.2&Aring;" />
caption="1fou, resolution 3.2&Aring;" />
'''CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29'''<br />
'''CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29'''<br />


==Overview==
==Overview==
Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of, bacterial viruses and certain animal viruses. Here we describe the motor, that packages the double-stranded DNA of the Bacillus subtilis, bacteriophage phi29 into a precursor capsid. We determined the structure, of the head-tail connector--the central component of the phi29 DNA, packaging motor--to 3.2 A resolution by means of X-ray crystallography. We, then fitted the connector into the electron densities of the prohead and, of the partially packaged prohead as determined using cryo-electron, microscopy and image reconstruction analysis. Our results suggest that the, prohead plus dodecameric connector, prohead RNA, viral ATPase and DNA, comprise a rotary motor with the head-prohead RNA-ATPase complex acting as, a stator, the DNA acting as a spindle, and the connector as a ball-race., The helical nature of the DNA converts the rotary action of the connector, into translation of the DNA.
Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we describe the motor that packages the double-stranded DNA of the Bacillus subtilis bacteriophage phi29 into a precursor capsid. We determined the structure of the head-tail connector--the central component of the phi29 DNA packaging motor--to 3.2 A resolution by means of X-ray crystallography. We then fitted the connector into the electron densities of the prohead and of the partially packaged prohead as determined using cryo-electron microscopy and image reconstruction analysis. Our results suggest that the prohead plus dodecameric connector, prohead RNA, viral ATPase and DNA comprise a rotary motor with the head-prohead RNA-ATPase complex acting as a stator, the DNA acting as a spindle, and the connector as a ball-race. The helical nature of the DNA converts the rotary action of the connector into translation of the DNA.


==About this Structure==
==About this Structure==
1FOU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FOU OCA].  
1FOU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_phage_f237 Vibrio phage f237]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FOU OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Vibrio phage f237]]
[[Category: Vibrio phage f237]]
[[Category: Anderson, D.L.]]
[[Category: Anderson, D L.]]
[[Category: Badasso, M.O.]]
[[Category: Badasso, M O.]]
[[Category: Baker, T.S.]]
[[Category: Baker, T S.]]
[[Category: Grimes, S.N.]]
[[Category: Grimes, S N.]]
[[Category: He, Y.]]
[[Category: He, Y.]]
[[Category: Jardine, P.J.]]
[[Category: Jardine, P J.]]
[[Category: Leiman, P.G.]]
[[Category: Leiman, P G.]]
[[Category: Morais, M.C.]]
[[Category: Morais, M C.]]
[[Category: Olson, N.H.]]
[[Category: Olson, N H.]]
[[Category: Rossmann, M.G.]]
[[Category: Rossmann, M G.]]
[[Category: Simpson, A.A.]]
[[Category: Simpson, A A.]]
[[Category: Tao, Y.]]
[[Category: Tao, Y.]]
[[Category: alpha-helical barrel]]
[[Category: alpha-helical barrel]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:06:10 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:58 2008''

Revision as of 13:41, 21 February 2008

File:1fou.gif


1fou, resolution 3.2Å

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CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29

OverviewOverview

Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we describe the motor that packages the double-stranded DNA of the Bacillus subtilis bacteriophage phi29 into a precursor capsid. We determined the structure of the head-tail connector--the central component of the phi29 DNA packaging motor--to 3.2 A resolution by means of X-ray crystallography. We then fitted the connector into the electron densities of the prohead and of the partially packaged prohead as determined using cryo-electron microscopy and image reconstruction analysis. Our results suggest that the prohead plus dodecameric connector, prohead RNA, viral ATPase and DNA comprise a rotary motor with the head-prohead RNA-ATPase complex acting as a stator, the DNA acting as a spindle, and the connector as a ball-race. The helical nature of the DNA converts the rotary action of the connector into translation of the DNA.

About this StructureAbout this Structure

1FOU is a Single protein structure of sequence from Vibrio phage f237. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the bacteriophage phi29 DNA packaging motor., Simpson AA, Tao Y, Leiman PG, Badasso MO, He Y, Jardine PJ, Olson NH, Morais MC, Grimes S, Anderson DL, Baker TS, Rossmann MG, Nature. 2000 Dec 7;408(6813):745-50. PMID:11130079

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