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| | ==The Solution Structure of gpV, the Major Tail Protein from Bacteriophage Lambda== | | ==The Solution Structure of gpV, the Major Tail Protein from Bacteriophage Lambda== |
| - | <StructureSection load='2k4q' size='340' side='right'caption='[[2k4q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2k4q' size='340' side='right'caption='[[2k4q]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2k4q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K4Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2k4q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K4Q FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">V ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Bacteriophage lambda])</td></tr> | + | </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=2k4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k4q OCA], [https://pdbe.org/2k4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k4q RCSB], [https://www.ebi.ac.uk/pdbsum/2k4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k4q 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=2k4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k4q OCA], [https://pdbe.org/2k4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k4q RCSB], [https://www.ebi.ac.uk/pdbsum/2k4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k4q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/VMTV_LAMBD VMTV_LAMBD]] Protein forming the phage's tail tube, which is composed of about 32 hexameric disks. There are 135-212 copies of gene V protein per mature phage. Probably undergoes structural rearrangements leading to injection of the phage DNA into the host (By similarity).
| + | [https://www.uniprot.org/uniprot/TUBE_LAMBD TUBE_LAMBD] Forms the phage's tail tube composed of 32 hexameric disks. When it encounters the appropriate initiation complex gpM and gpL, it assembles in hexameric rings that stack on top of each others. Multimerization ceases when the correct tail length is achieved through a mechanism dependent on tail terminator protein.<ref>PMID:2150582</ref> <ref>PMID:23911548</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacteriophage lambda]] | + | [[Category: Escherichia virus Lambda]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Davidson, A R]] | + | [[Category: Davidson AR]] |
| - | [[Category: Howell, P]] | + | [[Category: Howell P]] |
| - | [[Category: Kanelis, V]] | + | [[Category: Kanelis V]] |
| - | [[Category: Pell, L G]] | + | [[Category: Pell LG]] |
| - | [[Category: Gpv]]
| + | |
| - | [[Category: Major tail protein]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
TUBE_LAMBD Forms the phage's tail tube composed of 32 hexameric disks. When it encounters the appropriate initiation complex gpM and gpL, it assembles in hexameric rings that stack on top of each others. Multimerization ceases when the correct tail length is achieved through a mechanism dependent on tail terminator protein.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Most bacteriophages possess long tails, which serve as the conduit for genome delivery. We report the solution structure of the N-terminal domain of gpV, the protein comprising the major portion of the noncontractile phage lambda tail tube. This structure is very similar to a previously solved tail tube protein from a contractile-tailed phage, providing the first direct evidence of an evolutionary connection between these 2 distinct types of phage tails. A remarkable structural similarity is also seen to Hcp1, a component of the bacterial type VI secretion system. The hexameric structure of Hcp1 and its ability to form long tubes are strikingly reminiscent of gpV when it is polymerized into a tail tube. These data coupled with other similarities between phage and type VI secretion proteins support an evolutionary relationship between these systems. Using Hcp1 as a model, we propose a polymerization mechanism for gpV involving several disorder-to-order transitions.
The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system.,Pell LG, Kanelis V, Donaldson LW, Howell PL, Davidson AR Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4160-5. Epub 2009 Feb 27. PMID:19251647[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Katsura I. Mechanism of length determination in bacteriophage lambda tails. Adv Biophys. 1990;26:1-18. doi: 10.1016/0065-227x(90)90004-d. PMID:2150582 doi:http://dx.doi.org/10.1016/0065-227x(90)90004-d
- ↑ Xu J, Hendrix RW, Duda RL. Chaperone-protein interactions that mediate assembly of the bacteriophage lambda tail to the correct length. J Mol Biol. 2014 Mar 6;426(5):1004-18. doi: 10.1016/j.jmb.2013.06.040. Epub 2013 , Jul 30. PMID:23911548 doi:http://dx.doi.org/10.1016/j.jmb.2013.06.040
- ↑ Pell LG, Kanelis V, Donaldson LW, Howell PL, Davidson AR. The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4160-5. Epub 2009 Feb 27. PMID:19251647
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