1s2e

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(New page: 200px<br /><applet load="1s2e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s2e, resolution 2.30&Aring;" /> '''BACTERIOPHAGE T4 GEN...)
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[[Image:1s2e.jpg|left|200px]]<br /><applet load="1s2e" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1s2e, resolution 2.30&Aring;" />
'''BACTERIOPHAGE T4 GENE PRODUCT 9 (GP9), THE TRIGGER OF TAIL CONTRACTION AND THE LONG TAIL FIBERS CONNECTOR, ALTERNATIVE FIT OF THE FIRST 19 RESIDUES'''<br />
'''BACTERIOPHAGE T4 GENE PRODUCT 9 (GP9), THE TRIGGER OF TAIL CONTRACTION AND THE LONG TAIL FIBERS CONNECTOR, ALTERNATIVE FIT OF THE FIRST 19 RESIDUES'''<br />
==Overview==
==Overview==
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BACKGROUND: The T4 bacteriophage consists of a head, filled with, double-stranded DNA, and a complex contractile tail required for the, ejection of the viral genome into the Escherichia coli host. The tail has, a baseplate to which are attached six long and six short tail fibers., These fibers are the sensing devices for recognizing the host. When, activated by attachment to cell receptors, the fibers cause a, conformational transition in the baseplate and subsequently in the tail, sheath, which initiates DNA ejection. The baseplate is a multisubunit, complex of proteins encoded by 15 genes. Gene product 9 (gp9) is the, protein that connects the long tail fibers to the baseplate and triggers, the tail contraction after virus attachment to a host cell. RESULTS: The, crystal structure of recombinant gp9, determined to 2.3 A resolution, shows that the protein of 288 amino acid residues assembles as a, homotrimer. The monomer consists of three domains: the N-terminal domain, generates a triple coiled coil; the middle domain is a mixed, seven-stranded beta sandwich with a topology not previously observed; and, the C-terminal domain is an eight-stranded, antiparallel beta sandwich, having some resemblance to 'jelly-roll' viral capsid protein structures., CONCLUSIONS: The biologically active form of gp9 is a trimer. The protein, contains flexible interdomain hinges, which are presumably required to, facilitate signal transmission between the long tail fibers and the, baseplate. Structural and genetic analyses show that the C-terminal domain, is bound to the baseplate, and the N-terminal coiled-coil domain is, associated with the long tail fibers.
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BACKGROUND: The T4 bacteriophage consists of a head, filled with double-stranded DNA, and a complex contractile tail required for the ejection of the viral genome into the Escherichia coli host. The tail has a baseplate to which are attached six long and six short tail fibers. These fibers are the sensing devices for recognizing the host. When activated by attachment to cell receptors, the fibers cause a conformational transition in the baseplate and subsequently in the tail sheath, which initiates DNA ejection. The baseplate is a multisubunit complex of proteins encoded by 15 genes. Gene product 9 (gp9) is the protein that connects the long tail fibers to the baseplate and triggers the tail contraction after virus attachment to a host cell. RESULTS: The crystal structure of recombinant gp9, determined to 2.3 A resolution, shows that the protein of 288 amino acid residues assembles as a homotrimer. The monomer consists of three domains: the N-terminal domain generates a triple coiled coil; the middle domain is a mixed, seven-stranded beta sandwich with a topology not previously observed; and the C-terminal domain is an eight-stranded, antiparallel beta sandwich having some resemblance to 'jelly-roll' viral capsid protein structures. CONCLUSIONS: The biologically active form of gp9 is a trimer. The protein contains flexible interdomain hinges, which are presumably required to facilitate signal transmission between the long tail fibers and the baseplate. Structural and genetic analyses show that the C-terminal domain is bound to the baseplate, and the N-terminal coiled-coil domain is associated with the long tail fibers.
==About this Structure==
==About this Structure==
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1S2E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with EPE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S2E OCA].
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1S2E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2E OCA].
==Reference==
==Reference==
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[[Category: Bacteriophage t4]]
[[Category: Bacteriophage t4]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Kostyuchenko, V.A.]]
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[[Category: Kostyuchenko, V A.]]
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[[Category: Kurochkina, L.P.]]
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[[Category: Kurochkina, L P.]]
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[[Category: Mesyanzhinov, V.V.]]
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[[Category: Mesyanzhinov, V V.]]
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[[Category: Navruzbekov, G.A.]]
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[[Category: Navruzbekov, G A.]]
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[[Category: Rossmann, M.G.]]
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[[Category: Rossmann, M G.]]
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[[Category: Strelkov, S.V.]]
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[[Category: Strelkov, S V.]]
[[Category: EPE]]
[[Category: EPE]]
[[Category: bacteriophage t4]]
[[Category: bacteriophage t4]]
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[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:03:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:16 2008''

Revision as of 12:57, 21 February 2008


1s2e, resolution 2.30Å

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BACTERIOPHAGE T4 GENE PRODUCT 9 (GP9), THE TRIGGER OF TAIL CONTRACTION AND THE LONG TAIL FIBERS CONNECTOR, ALTERNATIVE FIT OF THE FIRST 19 RESIDUES

Overview

BACKGROUND: The T4 bacteriophage consists of a head, filled with double-stranded DNA, and a complex contractile tail required for the ejection of the viral genome into the Escherichia coli host. The tail has a baseplate to which are attached six long and six short tail fibers. These fibers are the sensing devices for recognizing the host. When activated by attachment to cell receptors, the fibers cause a conformational transition in the baseplate and subsequently in the tail sheath, which initiates DNA ejection. The baseplate is a multisubunit complex of proteins encoded by 15 genes. Gene product 9 (gp9) is the protein that connects the long tail fibers to the baseplate and triggers the tail contraction after virus attachment to a host cell. RESULTS: The crystal structure of recombinant gp9, determined to 2.3 A resolution, shows that the protein of 288 amino acid residues assembles as a homotrimer. The monomer consists of three domains: the N-terminal domain generates a triple coiled coil; the middle domain is a mixed, seven-stranded beta sandwich with a topology not previously observed; and the C-terminal domain is an eight-stranded, antiparallel beta sandwich having some resemblance to 'jelly-roll' viral capsid protein structures. CONCLUSIONS: The biologically active form of gp9 is a trimer. The protein contains flexible interdomain hinges, which are presumably required to facilitate signal transmission between the long tail fibers and the baseplate. Structural and genetic analyses show that the C-terminal domain is bound to the baseplate, and the N-terminal coiled-coil domain is associated with the long tail fibers.

About this Structure

1S2E is a Single protein structure of sequence from Bacteriophage t4 with as ligand. Full crystallographic information is available from OCA.

Reference

The structure of bacteriophage T4 gene product 9: the trigger for tail contraction., Kostyuchenko VA, Navruzbekov GA, Kurochkina LP, Strelkov SV, Mesyanzhinov VV, Rossmann MG, Structure. 1999 Oct 15;7(10):1213-22. PMID:10545330

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