1ox3
From Proteopedia
(New page: 200px<br /><applet load="1ox3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ox3, resolution 2.00Å" /> '''crystal structure of...) |
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| - | [[Image:1ox3.jpg|left|200px]]<br /><applet load="1ox3" size=" | + | [[Image:1ox3.jpg|left|200px]]<br /><applet load="1ox3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ox3, resolution 2.00Å" /> | caption="1ox3, resolution 2.00Å" /> | ||
'''crystal structure of mini-fibritin'''<br /> | '''crystal structure of mini-fibritin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Fibritin is a fibrous protein that forms "whiskers" attached to the neck | + | Fibritin is a fibrous protein that forms "whiskers" attached to the neck of bacteriophage T4. Whiskers interact with the long tail fibers regulating the assembly and infectivity of the virus. The fibritin trimer includes the N-terminal domain responsible for attachment to the phage particle and for the collar formation, the central domain forming a 500 A long segmented coiled-coil structure, and the C-terminal "foldon" domain. We have designed a "mini" fibritin with most of the coiled-coil domain deleted, and solved its crystal structure. The non-helical N-terminal part represents a new protein fold that tightly interacts with the coiled-coil segment forming a single domain, as revealed by calorimetry. The analysis of the crystal structure and earlier electron microscopy data on the collar-whisker complex suggests the necessity of other proteins to participate in the collar formation. Crystal structure determination of the N-terminal domain of fibritin is the first step towards elucidating the detailed structure and assembly mechanism of the collar-whisker complex. |
==About this Structure== | ==About this Structure== | ||
| - | 1OX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http:// | + | 1OX3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1OX3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Boudko, S | + | [[Category: Boudko, S P.]] |
[[Category: Stetefeld, J.]] | [[Category: Stetefeld, J.]] | ||
[[Category: capping motif]] | [[Category: capping motif]] | ||
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[[Category: foldon]] | [[Category: foldon]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:37 2008'' |
Revision as of 12:22, 21 February 2008
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crystal structure of mini-fibritin
Overview
Fibritin is a fibrous protein that forms "whiskers" attached to the neck of bacteriophage T4. Whiskers interact with the long tail fibers regulating the assembly and infectivity of the virus. The fibritin trimer includes the N-terminal domain responsible for attachment to the phage particle and for the collar formation, the central domain forming a 500 A long segmented coiled-coil structure, and the C-terminal "foldon" domain. We have designed a "mini" fibritin with most of the coiled-coil domain deleted, and solved its crystal structure. The non-helical N-terminal part represents a new protein fold that tightly interacts with the coiled-coil segment forming a single domain, as revealed by calorimetry. The analysis of the crystal structure and earlier electron microscopy data on the collar-whisker complex suggests the necessity of other proteins to participate in the collar formation. Crystal structure determination of the N-terminal domain of fibritin is the first step towards elucidating the detailed structure and assembly mechanism of the collar-whisker complex.
About this Structure
1OX3 is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
Reference
Design and crystal structure of bacteriophage T4 mini-fibritin NCCF., Boudko SP, Strelkov SV, Engel J, Stetefeld J, J Mol Biol. 2004 Jun 11;339(4):927-35. PMID:15165860
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