1tja

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(New page: 200px<br /><applet load="1tja" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tja" /> '''Fitting of gp8, gp9, and gp11 into the cryo-...)
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[[Image:1tja.gif|left|200px]]<br /><applet load="1tja" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1tja.gif|left|200px]]<br /><applet load="1tja" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1tja" />
caption="1tja" />
'''Fitting of gp8, gp9, and gp11 into the cryo-EM reconstruction of the bacteriophage T4 contracted tail'''<br />
'''Fitting of gp8, gp9, and gp11 into the cryo-EM reconstruction of the bacteriophage T4 contracted tail'''<br />
==Overview==
==Overview==
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The contractile tail of bacteriophage T4 undergoes major structural, transitions when the virus attaches to the host cell surface. The, baseplate at the distal end of the tail changes from a hexagonal to a star, shape. This causes the sheath around the tail tube to contract and the, tail tube to protrude from the baseplate and pierce the outer cell, membrane and the cell wall before reaching the inner cell membrane for, subsequent viral DNA injection. Analogously, the T4 tail can be contracted, by treatment with 3 M urea. The structure of the T4 contracted tail, including the head-tail joining region, has been determined by, cryo-electron microscopy to 17 A resolution. This 1200 A-long, 20 MDa, structure has been interpreted in terms of multiple copies of its, approximately 20 component proteins. A comparison with the metastable, hexagonal baseplate of the mature virus shows that the baseplate proteins, move as rigid bodies relative to each other during the structural change.
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The contractile tail of bacteriophage T4 undergoes major structural transitions when the virus attaches to the host cell surface. The baseplate at the distal end of the tail changes from a hexagonal to a star shape. This causes the sheath around the tail tube to contract and the tail tube to protrude from the baseplate and pierce the outer cell membrane and the cell wall before reaching the inner cell membrane for subsequent viral DNA injection. Analogously, the T4 tail can be contracted by treatment with 3 M urea. The structure of the T4 contracted tail, including the head-tail joining region, has been determined by cryo-electron microscopy to 17 A resolution. This 1200 A-long, 20 MDa structure has been interpreted in terms of multiple copies of its approximately 20 component proteins. A comparison with the metastable hexagonal baseplate of the mature virus shows that the baseplate proteins move as rigid bodies relative to each other during the structural change.
==About this Structure==
==About this Structure==
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1TJA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TJA OCA].
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1TJA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TJA OCA].
==Reference==
==Reference==
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[[Category: Bacteriophage t4]]
[[Category: Bacteriophage t4]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Chipman, P.R.]]
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[[Category: Chipman, P R.]]
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[[Category: Kostyuchenko, V.A.]]
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[[Category: Kostyuchenko, V A.]]
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[[Category: Leiman, P.G.]]
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[[Category: Leiman, P G.]]
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[[Category: Mesyanzhinov, V.V.]]
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[[Category: Mesyanzhinov, V V.]]
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[[Category: Rossmann, M.G.]]
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[[Category: Rossmann, M G.]]
[[Category: cryo-em]]
[[Category: cryo-em]]
[[Category: docking]]
[[Category: docking]]
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[[Category: gp9]]
[[Category: gp9]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:19:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:06 2008''

Revision as of 13:14, 21 February 2008


1tja

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Fitting of gp8, gp9, and gp11 into the cryo-EM reconstruction of the bacteriophage T4 contracted tail

Overview

The contractile tail of bacteriophage T4 undergoes major structural transitions when the virus attaches to the host cell surface. The baseplate at the distal end of the tail changes from a hexagonal to a star shape. This causes the sheath around the tail tube to contract and the tail tube to protrude from the baseplate and pierce the outer cell membrane and the cell wall before reaching the inner cell membrane for subsequent viral DNA injection. Analogously, the T4 tail can be contracted by treatment with 3 M urea. The structure of the T4 contracted tail, including the head-tail joining region, has been determined by cryo-electron microscopy to 17 A resolution. This 1200 A-long, 20 MDa structure has been interpreted in terms of multiple copies of its approximately 20 component proteins. A comparison with the metastable hexagonal baseplate of the mature virus shows that the baseplate proteins move as rigid bodies relative to each other during the structural change.

About this Structure

1TJA is a Protein complex structure of sequences from Bacteriophage t4. Full crystallographic information is available from OCA.

Reference

Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host., Leiman PG, Chipman PR, Kostyuchenko VA, Mesyanzhinov VV, Rossmann MG, Cell. 2004 Aug 20;118(4):419-29. PMID:15315755

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