1tja
From Proteopedia
(Difference between revisions)
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<SX load='1tja' size='340' side='right' viewer='molstar' caption='[[1tja]], [[Resolution|resolution]] 16.00Å' scene=''> | <SX load='1tja' size='340' side='right' viewer='molstar' caption='[[1tja]], [[Resolution|resolution]] 16.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1tja]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1tja]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TJA FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 16Å</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=1tja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tja OCA], [https://pdbe.org/1tja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tja RCSB], [https://www.ebi.ac.uk/pdbsum/1tja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tja 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=1tja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tja OCA], [https://pdbe.org/1tja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tja RCSB], [https://www.ebi.ac.uk/pdbsum/1tja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tja ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/BP08_BPT4 BP08_BPT4] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tja ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tja ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The contractile tail of bacteriophage T4 undergoes major structural transitions when the virus attaches to the host cell surface. The baseplate at the distal end of the tail changes from a hexagonal to a star shape. This causes the sheath around the tail tube to contract and the tail tube to protrude from the baseplate and pierce the outer cell membrane and the cell wall before reaching the inner cell membrane for subsequent viral DNA injection. Analogously, the T4 tail can be contracted by treatment with 3 M urea. The structure of the T4 contracted tail, including the head-tail joining region, has been determined by cryo-electron microscopy to 17 A resolution. This 1200 A-long, 20 MDa structure has been interpreted in terms of multiple copies of its approximately 20 component proteins. A comparison with the metastable hexagonal baseplate of the mature virus shows that the baseplate proteins move as rigid bodies relative to each other during the structural change. | ||
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- | Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host.,Leiman PG, Chipman PR, Kostyuchenko VA, Mesyanzhinov VV, Rossmann MG Cell. 2004 Aug 20;118(4):419-29. PMID:15315755<ref>PMID:15315755</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1tja" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
- | [[Category: | + | [[Category: Escherichia virus T4]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Chipman | + | [[Category: Chipman PR]] |
- | [[Category: Kostyuchenko | + | [[Category: Kostyuchenko VA]] |
- | [[Category: Leiman | + | [[Category: Leiman PG]] |
- | [[Category: Mesyanzhinov | + | [[Category: Mesyanzhinov VV]] |
- | [[Category: Rossmann | + | [[Category: Rossmann MG]] |
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Current revision
Fitting of gp8, gp9, and gp11 into the cryo-EM reconstruction of the bacteriophage T4 contracted tail
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