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 2.00&Aring;" /> '''crystal structure of...)
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[[Image:1ox3.jpg|left|200px]]<br /><applet load="1ox3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ox3, resolution 2.00&Aring;" />
 
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'''crystal structure of mini-fibritin'''<br />
 
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==Overview==
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==crystal structure of mini-fibritin==
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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.
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<StructureSection load='1ox3' size='340' side='right'caption='[[1ox3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ox3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OX3 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ox3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ox3 OCA], [https://pdbe.org/1ox3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ox3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ox3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ox3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/WAC_BPT4 WAC_BPT4] Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers').
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ox/1ox3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ox3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:15165860</ref>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OX3 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15165860 15165860]
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</div>
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[[Category: Bacteriophage t4]]
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<div class="pdbe-citations 1ox3" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Boudko, S.P.]]
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[[Category: Stetefeld, J.]]
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[[Category: capping motif]]
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[[Category: coiled coil]]
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[[Category: foldon]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:15:54 2007''
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==See Also==
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*[[Fibritin|Fibritin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia virus T4]]
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[[Category: Large Structures]]
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[[Category: Boudko SP]]
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[[Category: Stetefeld J]]

Current revision

crystal structure of mini-fibritin

PDB ID 1ox3

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