|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5iw9' size='340' side='right'caption='[[5iw9]], [[Resolution|resolution]] 2.47Å' scene=''> | | <StructureSection load='5iw9' size='340' side='right'caption='[[5iw9]], [[Resolution|resolution]] 2.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5iw9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4hrz 4hrz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IW9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5IW9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5iw9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4hrz 4hrz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IW9 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.47Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5iw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iw9 OCA], [http://pdbe.org/5iw9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iw9 RCSB], [http://www.ebi.ac.uk/pdbsum/5iw9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iw9 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=5iw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iw9 OCA], [https://pdbe.org/5iw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iw9 RCSB], [https://www.ebi.ac.uk/pdbsum/5iw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iw9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BP25_BPT4 BP25_BPT4]] Baseplate protein that is part of the outer wedges of the baseplate (PubMed:15315755). Probably plays a role as a connector between the central and peripheral parts of the baseplate. Involved in the tail assembly.[UniProtKB:P51768]<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> | + | [https://www.uniprot.org/uniprot/BP25_BPT4 BP25_BPT4] Baseplate protein that is part of the outer wedges of the baseplate (PubMed:15315755). Probably plays a role as a connector between the central and peripheral parts of the baseplate. Involved in the tail assembly.[UniProtKB:P51768]<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpt4]] | + | [[Category: Escherichia virus T4]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Browning, C]] | + | [[Category: Browning C]] |
| - | [[Category: Leiman, P G]] | + | [[Category: Leiman PG]] |
| - | [[Category: Shneider, M M]] | + | [[Category: Shneider MM]] |
| - | [[Category: Baseplate]]
| + | |
| - | [[Category: Contractile sheath]]
| + | |
| - | [[Category: Sheath polymerization]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Wedge]]
| + | |
| Structural highlights
Function
BP25_BPT4 Baseplate protein that is part of the outer wedges of the baseplate (PubMed:15315755). Probably plays a role as a connector between the central and peripheral parts of the baseplate. Involved in the tail assembly.[UniProtKB:P51768][1] [2]
Publication Abstract from PubMed
Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.
Structure of the T4 baseplate and its function in triggering sheath contraction.,Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971. PMID:27193680[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leiman PG, Chipman PR, Kostyuchenko VA, Mesyanzhinov VV, Rossmann MG. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell. 2004 Aug 20;118(4):419-29. PMID:15315755 doi:10.1016/j.cell.2004.07.022
- ↑ Leiman PG, Arisaka F, van Raaij MJ, Kostyuchenko VA, Aksyuk AA, Kanamaru S, Rossmann MG. Morphogenesis of the T4 tail and tail fibers. Virol J. 2010 Dec 3;7:355. doi: 10.1186/1743-422X-7-355. PMID:21129200 doi:10.1186/1743-422X-7-355
- ↑ Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG. Structure of the T4 baseplate and its function in triggering sheath contraction. Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971. PMID:27193680 doi:http://dx.doi.org/10.1038/nature17971
|
