1ox3
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(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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Revision as of 21:08, 20 November 2007
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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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