1cd3: Difference between revisions

New page: left|200px<br /> <applet load="1cd3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cd3, resolution 3.5Å" /> '''PROCAPSID OF BACTERI...
 
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[[Image:1cd3.gif|left|200px]]<br />
<applet load="1cd3" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cd3, resolution 3.5&Aring;" />
'''PROCAPSID OF BACTERIOPHAGE PHIX174'''<br />


==Overview==
==PROCAPSID OF BACTERIOPHAGE PHIX174==
An empty precursor particle called the procapsid is formed during assembly, of the single-stranded DNA bacteriophage phiX174. Assembly of the phiX174, procapsid requires the presence of the two scaffolding proteins, D and B, which are structural components of the procapsid, but are not found in the, mature virion. The X-ray crystallographic structure of a "closed", procapsid particle has been determined to 3.5 A resolution. This structure, has an external scaffold made from 240 copies of protein D, 60 copies of, the internally located B protein, and contains 60 copies of each of the, viral structural proteins F and G, which comprise the shell and the 5-fold, spikes, respectively. The F capsid protein has a similar conformation to, that seen in the mature virion, and differs from the previously determined, 25 A resolution electron microscopic reconstruction of the "open", procapsid, in which the F protein has a different conformation. The D, scaffolding protein has a predominantly alpha-helical fold and displays, remarkable conformational variability. We report here an improved and, refined structure of the closed procapsid and describe in some detail the, differences between the four independent D scaffolding proteins per, icosahedral asymmetric unit, as well as their interaction with the F, capsid protein. We re-analyze and correct the comparison of the closed, procapsid with the previously determined cryo-electron microscopic image, reconstruction of the open procapsid and discuss the major structural, rearrangements that must occur during assembly. A model is proposed in, which the D proteins direct the assembly process by sequential binding and, conformational switching.
<StructureSection load='1cd3' size='340' side='right'caption='[[1cd3]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1cd3]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_phiX174 Escherichia virus phiX174]. The February 2000 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Bacteriophage phiX174''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2000_2 10.2210/rcsb_pdb/mom_2000_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CD3 FirstGlance]. <br>
1CD3 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_phix174 Enterobacteria phage phix174]. The following page contains interesting information on the relation of 1CD3 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb2_1.html Bacteriophage phiX174]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CD3 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cd3 OCA], [https://pdbe.org/1cd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cd3 RCSB], [https://www.ebi.ac.uk/pdbsum/1cd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cd3 ProSAT]</span></td></tr>
==Reference==
</table>
The role of scaffolding proteins in the assembly of the small, single-stranded DNA virus phiX174., Dokland T, Bernal RA, Burch A, Pletnev S, Fane BA, Rossmann MG, J Mol Biol. 1999 May 14;288(4):595-608. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10329166 10329166]
== Function ==
[https://www.uniprot.org/uniprot/CAPSD_BPPHS CAPSD_BPPHS] Assembles to form an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins F (PubMed:11991963, PubMed:1370343, PubMed:8158636). Upon virus binding to host cell, one of the spikes dissociates from the capsid and the virus interacts with LPS through the exposed EF loops on the F proteins (PubMed:29229840). After the genome had been ejected, the channel formed by the F proteins at the unique fivefold axis remains open (PubMed:29229840).<ref>PMID:11991963</ref> <ref>PMID:1370343</ref> <ref>PMID:29229840</ref> <ref>PMID:8158636</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cd/1cd3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1cd3 ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteriophage phiX174]]
[[Category: Bacteriophage phiX174]]
[[Category: Enterobacteria phage phix174]]
[[Category: Escherichia virus phiX174]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Dokland, T.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Rossmann, M.G.]]
[[Category: Dokland T]]
[[Category: bacteriophage]]
[[Category: Rossmann MG]]
[[Category: chaperone]]
[[Category: complex (virus capsid proteins)]]
[[Category: icosahedral virus]]
[[Category: procapsid]]
[[Category: scaffolding protein]]
 
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