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| | ==Crystal structure of the pre-mature bacteriophage phi29 gene product 12== | | ==Crystal structure of the pre-mature bacteriophage phi29 gene product 12== |
| - | <StructureSection load='3suc' size='340' side='right' caption='[[3suc]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='3suc' size='340' side='right'caption='[[3suc]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3suc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpph2 Bpph2]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gqn 3gqn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SUC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SUC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3suc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_virus_phi29 Bacillus virus phi29]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3gqn 3gqn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SUC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3gqn|3gqn]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">12 ([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=3suc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3suc OCA], [https://pdbe.org/3suc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3suc RCSB], [https://www.ebi.ac.uk/pdbsum/3suc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3suc ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3suc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3suc OCA], [http://pdbe.org/3suc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3suc RCSB], [http://www.ebi.ac.uk/pdbsum/3suc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3suc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FIB12_BPPH2 FIB12_BPPH2] Structural component of the 12 appendages that hang from the lower collar. Adhesion protein that binds to the host cell surface during virus attachment and mediates teichoic acids degradation.<ref>PMID:7241648</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: Rossmann, M G]] | + | [[Category: Large Structures]] |
| - | [[Category: Xiang, Y]] | + | [[Category: Rossmann MG]] |
| - | [[Category: Atp binding]] | + | [[Category: Xiang Y]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Beta helix]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
FIB12_BPPH2 Structural component of the 12 appendages that hang from the lower collar. Adhesion protein that binds to the host cell surface during virus attachment and mediates teichoic acids degradation.[1]
Publication Abstract from PubMed
The tailed bacteriophage phi29 has 12 "appendages" (gene product 12, gp12) attached to its neck region that participate in host cell recognition and entry. In the cell, monomeric gp12 undergoes proteolytic processing that releases the C-terminal domain during assembly into trimers. We report here crystal structures of the protein before and after catalytic processing and show that the C-terminal domain of gp12 is an "autochaperone" that aids trimerization. We also show that autocleavage of the C-terminal domain is a posttrimerization event that is followed by a unique ATP-dependent release. The posttranslationally modified N-terminal part has three domains that function to attach the appendages to the phage, digest the cell wall teichoic acids, and bind irreversibly to the host, respectively. Structural and sequence comparisons suggest that some eukaryotic and bacterial viruses as well as bacterial adhesins might have a similar maturation mechanism as is performed by phi29 gp12 for Bacillus subtilis.
Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike.,Xiang Y, Leiman PG, Li L, Grimes S, Anderson DL, Rossmann MG Mol Cell. 2009 May 15;34(3):375-86. PMID:19450535[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Villanueva N, Salas M. Adsorption of bacteriophage phi 29 to Bacillus subtilis through the neck appendages of the viral particle. J Virol. 1981 Apr;38(1):15-9. PMID:7241648
- ↑ Xiang Y, Leiman PG, Li L, Grimes S, Anderson DL, Rossmann MG. Crystallographic insights into the autocatalytic assembly mechanism of a bacteriophage tail spike. Mol Cell. 2009 May 15;34(3):375-86. PMID:19450535 doi:10.1016/j.molcel.2009.04.009
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