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| | ==The crystal structure of the C-terminal domain of Mu phage central spike - Pt derivative for MAD== | | ==The crystal structure of the C-terminal domain of Mu phage central spike - Pt derivative for MAD== |
| - | <StructureSection load='3vtn' size='340' side='right' caption='[[3vtn]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='3vtn' size='340' side='right'caption='[[3vtn]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vtn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpmu Bpmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VTN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vtn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpmu Bpmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VTN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vto|3vto]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vto|3vto]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">45 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 BPMU])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">45 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 BPMU])</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=3vtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vtn OCA], [http://pdbe.org/3vtn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vtn RCSB], [http://www.ebi.ac.uk/pdbsum/3vtn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vtn ProSAT]</span></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=3vtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vtn OCA], [https://pdbe.org/3vtn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vtn RCSB], [https://www.ebi.ac.uk/pdbsum/3vtn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vtn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BP45_BPMU BP45_BPMU]] Component of the baseplate that forms a central needlelike spike used to puncture the host cell membrane for tube insertion during virus entry. Probably involved in baseplate and tail assembly. Serves as the distal plug of tail tube channel and might regulate the process of the phage DNA and protein ejection into the host cell.<ref>PMID:20478417</ref> <ref>PMID:22922659</ref> | + | [[https://www.uniprot.org/uniprot/BP45_BPMU BP45_BPMU]] Component of the baseplate that forms a central needlelike spike used to puncture the host cell membrane for tube insertion during virus entry. Probably involved in baseplate and tail assembly. Serves as the distal plug of tail tube channel and might regulate the process of the phage DNA and protein ejection into the host cell.<ref>PMID:20478417</ref> <ref>PMID:22922659</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Bpmu]] | | [[Category: Bpmu]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Harada, K]] | | [[Category: Harada, K]] |
| | [[Category: Nakagawa, A]] | | [[Category: Nakagawa, A]] |
| Structural highlights
Function
[BP45_BPMU] Component of the baseplate that forms a central needlelike spike used to puncture the host cell membrane for tube insertion during virus entry. Probably involved in baseplate and tail assembly. Serves as the distal plug of tail tube channel and might regulate the process of the phage DNA and protein ejection into the host cell.[1] [2]
Publication Abstract from PubMed
Bacteriophage Mu, which has a contractile tail, is one of the most famous genus of Myoviridae. It has a wide host range and is thought to contribute to horizontal gene transfer. The Myoviridae infection process is initiated by adhesion to the host surface. The phage then penetrates the host cell membrane using its tail to inject its genetic material into the host. In this penetration process, Myoviridae phages are proposed to puncture the membrane of the host cell using a central spike located beneath its baseplate. The central spike of the Mu phage is thought to be composed of gene 45 product (gp45), which has a significant sequence homology with the central spike of P2 phage (gpV). We determined the crystal structure of shortened Mu gp45Delta1-91 (Arg92-Gln197) at 1.5A resolution and showed that Mu gp45 is a needlelike structure that punctures the membrane. The apex of Mu gp45 and that of P2 gpV contained iron, chloride, and calcium ions. Although the C-terminal domain of Mu gp45 was sufficient for binding to the E. coli membrane, a mutant D188A, in which the Asp amino acid residue that coordinates the calcium ion was replaced by Ala, did not exhibit a propensity to bind to the membrane. Therefore, we concluded that calcium ion played an important role in interaction with the host cell membrane.
Crystal structure of the C-terminal domain of Mu phage central spike and functions of bound calcium ion.,Harada K, Yamashita E, Nakagawa A, Miyafusa T, Tsumoto K, Ueno T, Toyama Y, Takeda S Biochim Biophys Acta. 2013 Jan;1834(1):284-91. doi: 10.1016/j.bbapap.2012.08.015., Epub 2012 Aug 24. PMID:22922659[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Suzuki H, Yamada S, Toyama Y, Takeda S. The C-terminal domain is sufficient for host-binding activity of the Mu phage tail-spike protein. Biochim Biophys Acta. 2010 Sep;1804(9):1738-42. doi:, 10.1016/j.bbapap.2010.05.003. Epub 2010 May 15. PMID:20478417 doi:http://dx.doi.org/10.1016/j.bbapap.2010.05.003
- ↑ Harada K, Yamashita E, Nakagawa A, Miyafusa T, Tsumoto K, Ueno T, Toyama Y, Takeda S. Crystal structure of the C-terminal domain of Mu phage central spike and functions of bound calcium ion. Biochim Biophys Acta. 2013 Jan;1834(1):284-91. doi: 10.1016/j.bbapap.2012.08.015., Epub 2012 Aug 24. PMID:22922659 doi:http://dx.doi.org/10.1016/j.bbapap.2012.08.015
- ↑ Harada K, Yamashita E, Nakagawa A, Miyafusa T, Tsumoto K, Ueno T, Toyama Y, Takeda S. Crystal structure of the C-terminal domain of Mu phage central spike and functions of bound calcium ion. Biochim Biophys Acta. 2013 Jan;1834(1):284-91. doi: 10.1016/j.bbapap.2012.08.015., Epub 2012 Aug 24. PMID:22922659 doi:http://dx.doi.org/10.1016/j.bbapap.2012.08.015
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