1al0: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1al0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1al0, resolution 3.5Å" /> '''PROCAPSID OF BACTERIO...
 
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1al0.gif|left|200px]]<br /><applet load="1al0" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1al0, resolution 3.5&Aring;" />
'''PROCAPSID OF BACTERIOPHAGE PHIX174'''<br />


==Overview==
==PROCAPSID OF BACTERIOPHAGE PHIX174==
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.
<StructureSection load='1al0' size='340' side='right'caption='[[1al0]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
1AL0 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]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AL0 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=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>
==Reference==
</table>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9305849 9305849]
== Function ==
[[Category: Enterobacteria phage 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>
[[Category: Protein complex]]
== Evolutionary Conservation ==
[[Category: Dokland, T.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Rossmann, M.G.]]
Check<jmol>
[[Category: bacteriophage]]
  <jmolCheckbox>
[[Category: chaperone]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/al/1al0_consurf.spt"</scriptWhenChecked>
[[Category: complex (virus capsid proteins)]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: icosahedral virus]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: procapsid]]
  </jmolCheckbox>
[[Category: scaffolding protein]]
</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].
 
<div style="clear:both"></div>
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:56:14 2007''
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia virus phiX174]]
[[Category: Large Structures]]
[[Category: Dokland T]]
[[Category: Rossmann MG]]

Latest revision as of 09:31, 7 February 2024

PROCAPSID OF BACTERIOPHAGE PHIX174PROCAPSID OF BACTERIOPHAGE PHIX174

Structural highlights

1al0 is a 7 chain structure with sequence from Escherichia virus phiX174. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Uchiyama A, Fane BA. Identification of an interacting coat-external scaffolding protein domain required for both the initiation of phiX174 procapsid morphogenesis and the completion of DNA packaging. J Virol. 2005 Jun;79(11):6751-6. PMID:15890913 doi:http://dx.doi.org/10.1128/JVI.79.11.6751-6756.2005
  2. ↑ Mukai R, Hamatake RK, Hayashi M. Isolation and identification of bacteriophage phi X174 prohead. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4877-81. PMID:159449

1al0, resolution 3.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1al0&oldid=4040215"