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| | <StructureSection load='1noh' size='340' side='right'caption='[[1noh]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='1noh' size='340' side='right'caption='[[1noh]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1noh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpph2 Bpph2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NOH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1noh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NOH 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;'>[[1no4|1no4]]</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]] 2.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gp7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10756 BPPH2])</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=1noh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1noh OCA], [https://pdbe.org/1noh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1noh RCSB], [https://www.ebi.ac.uk/pdbsum/1noh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1noh 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=1noh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1noh OCA], [http://pdbe.org/1noh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1noh RCSB], [http://www.ebi.ac.uk/pdbsum/1noh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1noh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SCAF_BPPH2 SCAF_BPPH2] Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are released from the procapsid.<ref>PMID:17098197</ref> <ref>PMID:17198713</ref> <ref>PMID:23896641</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpph2]] | + | [[Category: Bacillus virus phi29]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Anderson, D L]] | + | [[Category: Badasso MO]] |
| - | [[Category: Badasso, M O]] | + | [[Category: Kanamaru S]] |
| - | [[Category: Kanamaru, S]] | + | [[Category: Koti JS]] |
| - | [[Category: Koti, J S]] | + | [[Category: L Anderson D]] |
| - | [[Category: McMurray, C T]] | + | [[Category: McMurray CT]] |
| - | [[Category: Morais, M C]] | + | [[Category: Morais MC]] |
| - | [[Category: Owen, B L]] | + | [[Category: Owen BL]] |
| - | [[Category: Rossmann, M G]] | + | [[Category: Rossmann MG]] |
| - | [[Category: Coiled-coil]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
SCAF_BPPH2 Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are released from the procapsid.[1] [2] [3]
Publication Abstract from PubMed
Three-dimensional structures of the double-stranded DNA bacteriophage phi29 scaffolding protein (gp7) before and after prohead assembly have been determined at resolutions of 2.2 and 2.8 A, respectively. Both structures are dimers that resemble arrows, with a four-helix bundle composing the arrowhead and a coiled coil forming the tail. The structural resemblance of gp7 to the yeast transcription factor GCN4 suggests a DNA-binding function that was confirmed by native gel electrophoresis. DNA binding to gp7 may have a role in mediating the structural transition from prohead to mature virus and scaffold release. A cryo-EM analysis indicates that gp7 is arranged inside the capsid as a series of concentric shells. The position of the higher density features in these shells correlates with the positions of hexamers in the equatorial region of the capsid, suggesting that gp7 may regulate formation of the prolate head through interactions with these hexamers.
Bacteriophage phi29 scaffolding protein gp7 before and after prohead assembly.,Morais MC, Kanamaru S, Badasso MO, Koti JS, Owen BA, McMurray CT, Anderson DL, Rossmann MG Nat Struct Biol. 2003 Jul;10(7):572-6. PMID:12778115[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Choi KH, Morais MC, Anderson DL, Rossmann MG. Determinants of bacteriophage phi29 head morphology. Structure. 2006 Nov;14(11):1723-7. PMID:17098197 doi:http://dx.doi.org/10.1016/j.str.2006.09.007
- ↑ Fu CY, Morais MC, Battisti AJ, Rossmann MG, Prevelige PE Jr. Molecular dissection of o29 scaffolding protein function in an in vitro assembly system. J Mol Biol. 2007 Mar 2;366(4):1161-73. Epub 2006 Dec 6. PMID:17198713 doi:http://dx.doi.org/10.1016/j.jmb.2006.11.091
- ↑ Li R, Cherwa JE Jr, Prevelige PE Jr. varphi29 Scaffolding and connector structure-function relationship studied by trans-complementation. Virology. 2013 Sep;444(1-2):355-62. doi: 10.1016/j.virol.2013.07.001. Epub 2013, Jul 27. PMID:23896641 doi:http://dx.doi.org/10.1016/j.virol.2013.07.001
- ↑ Morais MC, Kanamaru S, Badasso MO, Koti JS, Owen BA, McMurray CT, Anderson DL, Rossmann MG. Bacteriophage phi29 scaffolding protein gp7 before and after prohead assembly. Nat Struct Biol. 2003 Jul;10(7):572-6. PMID:12778115 doi:10.1038/nsb939
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