2l04: Difference between revisions

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 ==The Solution Structure of the C-terminal Ig-like Domain of the Bacteriophage Lambda Tail Tube Protein==
-<StructureSection load='2l04' size='340' side='right'caption='[[2l04]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2l04' size='340' side='right'caption='[[2l04]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l04]] 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=2L04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L04 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l04]] 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=2L04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L04 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2l04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l04 OCA], [https://pdbe.org/2l04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l04 RCSB], [https://www.ebi.ac.uk/pdbsum/2l04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l04 ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[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=2l04 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Immunoglobulin (Ig)-like domains are found frequently on the surface of tailed double-stranded DNA bacteriophages, yet their functional role remains obscure. Here, we have investigated the structure and function of the C-terminal Ig-like domain of gpV (gpV(C)), the tail tube protein of phage lambda. This domain has been predicted through sequence similarity to be a member of the bacterial Ig-like domain 2 (Big_2) family, which is composed of more than 1300 phage and bacterial sequences. Using trypsin proteolysis, we have delineated the boundaries of gpV(C) and have shown that its removal reduces the biological activity of gpV by 100-fold; thus providing a definitive demonstration of a functional role for this domain. Determination of the solution structure of gpV(C) by NMR spectroscopy showed that it adopts a canonical Ig-like fold of the I-set class. This represents the first structure of a phage-encoded Ig-like domain and only the second structure of a Big_2 domain. Structural and sequence comparisons indicate that the gpV(C) structure is more representative of both the phage-encoded Big_2 domains and Big_2 domains in general than the other available Big_2 structure. Bioinformatics analyses have identified two conserved clusters of residues on the surface of gpV(C) that may be important in mediating the function of this domain.
-The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage lambda Tail Tube Protein.,Pell LG, Gasmi-Seabrook GM, Morais M, Neudecker P, Kanelis V, Bona D, Donaldson LW, Edwards AM, Howell PL, Davidson AR, Maxwell KL J Mol Biol. 2010 Sep 6. PMID:20826161<ref>PMID:20826161</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2l04" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacteriophage lambda]]
+[[Category: Escherichia virus Lambda]]
 [[Category: Large Structures]]
-[[Category: Davidson, A R]]
+[[Category: Davidson AR]]
-[[Category: Donaldson, L W]]
+[[Category: Donaldson LW]]
-[[Category: Gasmi-Seabrook, G M.C]]
+[[Category: Gasmi-Seabrook GMC]]
-[[Category: Howell, P]]
+[[Category: Howell P]]
-[[Category: Maxwell, K L]]
+[[Category: Maxwell KL]]
-[[Category: Pell, L G]]
+[[Category: Pell LG]]
-[[Category: Gpv]]
-[[Category: Ig-like domain]]
-[[Category: Phage tail]]
-[[Category: Viral protein]]