1al0: Difference between revisions

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[[Image:1al0.gif|left|200px]]


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==PROCAPSID OF BACTERIOPHAGE PHIX174==
The line below this paragraph, containing "STRUCTURE_1al0", creates the "Structure Box" on the page.
<StructureSection load='1al0' size='340' side='right'caption='[[1al0]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1al0]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_phiX174 Escherichia virus phiX174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AL0 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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=1al0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al0 OCA], [https://pdbe.org/1al0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1al0 RCSB], [https://www.ebi.ac.uk/pdbsum/1al0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1al0 ProSAT]</span></td></tr>
{{STRUCTURE_1al0|  PDB=1al0  |  SCENE= }}
</table>
 
== Function ==
'''PROCAPSID OF BACTERIOPHAGE PHIX174'''
[https://www.uniprot.org/uniprot/SCAFD_BPPHS SCAFD_BPPHS] Assembles the procapsid by joining twelve 12S pre-assembly complex into a T=1 icosahedral particle, called 108S procapsid. Ten proteins D bind each 12S complex, which are formed by three pentamers of F, G, B protein and a H protein. The scaffolding protein is released from the provirion after genome packaging to form the mature virion.<ref>PMID:15890913</ref> <ref>PMID:159449</ref>
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
The assembly of a macromolecular structure proceeds along an ordered morphogenetic pathway, and is accomplished by the switching of proteins between discrete conformations as they are added to the nascent assembly. Scaffolding proteins often play a catalytic role in the assembly process, rather like molecular chaperones. Although macromolecular assembly processes are fundamental to all biological systems, they have been characterized most thoroughly in viral systems, such as the icosahedral Escherichia coli bacteriophage phiX174. The phiX174 virion contains the proteins F, G, H and J. During assembly, two scaffoldingproteins B and D are required for the formation of a 108S, 360-A-diameter procapsid from pentameric precursors containing the F, G and H proteins. The procapsid contains 240 copies of protein D, forming an external scaffold, and 60 copies each of the internal scaffolding protein B, the capsid protein F, and the spike protein G. Maturation involves packaging of DNA and J proteins and loss of protein B, producing a 132S intermediate. Subsequent removal of the external scaffold yields the mature virion. Both the F and G proteins have the eight-stranded antiparallel beta-sandwich motif common to many plant and animal viruses. Here we describe the structure of a procapsid-like particle at 3.5-A resolution, showing how the scaffolding proteins coordinate assembly of the virus by interactions with the F and G proteins, and showing that the F protein undergoes conformational changes during capsid maturation.
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/al/1al0_consurf.spt"</scriptWhenChecked>
==About this Structure==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
1AL0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_phix174 Enterobacteria phage phix174]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AL0 OCA].  
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==Reference==
</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=1al0 ConSurf].
Structure of a viral procapsid with molecular scaffolding., Dokland T, McKenna R, Ilag LL, Bowman BR, Incardona NL, Fane BA, Rossmann MG, Nature. 1997 Sep 18;389(6648):308-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9305849 9305849]
<div style="clear:both"></div>
[[Category: Enterobacteria phage phix174]]
== References ==
[[Category: Protein complex]]
<references/>
[[Category: Dokland, T.]]
__TOC__
[[Category: Rossmann, M G.]]
</StructureSection>
[[Category: Bacteriophage]]
[[Category: Escherichia virus phiX174]]
[[Category: Chaperone]]
[[Category: Large Structures]]
[[Category: Icosahedral virus]]
[[Category: Dokland T]]
[[Category: Procapsid]]
[[Category: Rossmann MG]]
[[Category: Scaffolding protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:24:26 2008''

Latest revision as of 06:31, 7 February 2024

PROCAPSID OF BACTERIOPHAGE PHIX174

1al0, resolution 3.50Å

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