1al0

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[[Image:1al0.gif|left|200px]]
 
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{{Structure
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==PROCAPSID OF BACTERIOPHAGE PHIX174==
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|PDB= 1al0 |SIZE=350|CAPTION= <scene name='initialview01'>1al0</scene>, resolution 3.5&Aring;
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<StructureSection load='1al0' size='340' side='right'caption='[[1al0]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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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]] 3.5&#8491;</td></tr>
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|GENE=
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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=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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1al0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al0 OCA], [http://www.ebi.ac.uk/pdbsum/1al0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1al0 RCSB]</span>
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[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>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''PROCAPSID OF BACTERIOPHAGE PHIX174'''
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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/al/1al0_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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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.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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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=1al0 ConSurf].
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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].
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<div style="clear:both"></div>
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== References ==
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==Reference==
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<references/>
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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]
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__TOC__
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[[Category: Enterobacteria phage phix174]]
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</StructureSection>
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[[Category: Protein complex]]
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[[Category: Escherichia virus phiX174]]
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[[Category: Dokland, T.]]
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[[Category: Large Structures]]
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[[Category: Rossmann, M G.]]
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[[Category: Dokland T]]
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[[Category: bacteriophage]]
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[[Category: Rossmann MG]]
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[[Category: chaperone]]
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[[Category: complex (virus capsid proteins)]]
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[[Category: icosahedral virus]]
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[[Category: procapsid]]
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[[Category: scaffolding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:42:29 2008''
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Current revision

PROCAPSID OF BACTERIOPHAGE PHIX174

PDB ID 1al0

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