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| | <StructureSection load='1tx9' size='340' side='right'caption='[[1tx9]], [[Resolution|resolution]] 3.31Å' scene=''> | | <StructureSection load='1tx9' size='340' side='right'caption='[[1tx9]], [[Resolution|resolution]] 3.31Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1tx9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpphx Bpphx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TX9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TX9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1tx9]] is a 2 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=1TX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TX9 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cd3|1cd3]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.31Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10847 BPPHX])</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=1tx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tx9 OCA], [https://pdbe.org/1tx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tx9 RCSB], [https://www.ebi.ac.uk/pdbsum/1tx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tx9 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1tx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tx9 OCA], [http://pdbe.org/1tx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tx9 RCSB], [http://www.ebi.ac.uk/pdbsum/1tx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tx9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/D_BPPHX D_BPPHX]] 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:159449</ref> <ref>PMID:15890913</ref> | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpphx]] | + | [[Category: Escherichia virus phiX174]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fane, B A]] | + | [[Category: Fane BA]] |
| - | [[Category: Fisher, M]] | + | [[Category: Fisher M]] |
| - | [[Category: Kanamaru, K]] | + | [[Category: Kanamaru K]] |
| - | [[Category: Morais, M C]] | + | [[Category: Morais MC]] |
| - | [[Category: Rossmann, M G]] | + | [[Category: Rossmann MG]] |
| - | [[Category: Assembly]]
| + | |
| - | [[Category: Conformational switching]]
| + | |
| - | [[Category: Phix174]]
| + | |
| - | [[Category: Scaffolding protein]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
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.
Publication Abstract from PubMed
The three-dimensional structure of bacteriophage phiX174 external scaffolding protein D, prior to its interaction with other structural proteins, has been determined to 3.3 angstroms by X-ray crystallography. The crystals belong to space group P4(1)2(1)2 with a dimer in the asymmetric unit that closely resembles asymmetric dimers observed in the phiX174 procapsid structure. Furthermore, application of the crystallographic 4(1) symmetry operation to one of these dimers generates a tetramer similar to the tetramer in the icosahedral asymmetric unit of the procapsid. These data suggest that both dimers and tetramers of the D protein are true morphogenetic intermediates and can form independently of other proteins involved in procapsid morphogenesis. The crystal structure of the D scaffolding protein thus represents the state of the polypeptide prior to procapsid assembly. Hence, comparison with the procapsid structure provides a rare opportunity to follow the conformational switching events necessary for the construction of complex macromolecular assemblies.
Conformational switching by the scaffolding protein D directs the assembly of bacteriophage phiX174.,Morais MC, Fisher M, Kanamaru S, Przybyla L, Burgner J, Fane BA, Rossmann MG Mol Cell. 2004 Sep 24;15(6):991-7. PMID:15383287[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
- ↑ 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
- ↑ Morais MC, Fisher M, Kanamaru S, Przybyla L, Burgner J, Fane BA, Rossmann MG. Conformational switching by the scaffolding protein D directs the assembly of bacteriophage phiX174. Mol Cell. 2004 Sep 24;15(6):991-7. PMID:15383287 doi:10.1016/j.molcel.2004.08.023
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