3h2t: Difference between revisions

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OCA

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 ==Crystal structure of gene product 6, baseplate protein of bacteriophage T4==
-<StructureSection load='3h2t' size='340' side='right' caption='[[3h2t]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+<StructureSection load='3h2t' size='340' side='right'caption='[[3h2t]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3h2t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H2T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3h2t]] is a 2 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=3H2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H2T FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">6, gene 6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</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]] 3.2&#8491;</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=3h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h2t OCA], [http://pdbe.org/3h2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h2t RCSB], [http://www.ebi.ac.uk/pdbsum/3h2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h2t 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=3h2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h2t OCA], [https://pdbe.org/3h2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h2t RCSB], [https://www.ebi.ac.uk/pdbsum/3h2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h2t ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/BP06_BPT4 BP06_BPT4] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/3h2t_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h2/3h2t_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 17: / Line 19: @@
 </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=3h2t ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The baseplate of bacteriophage T4 is a multicomponent protein complex, which controls phage attachment to the host. It assembles from six wedges and a central hub. During infection the baseplate undergoes a large conformational change from a dome-shaped to a flat, star-shaped structure. We report the crystal structure of the C-terminal half of gene product (gp) 6 and investigate its motion with respect to the other proteins during the baseplate rearrangement. Six gp6 dimers interdigitate, forming a ring that maintains the integrity of the baseplate in both conformations. One baseplate wedge contains an N-terminal dimer of gp6, whereas neighboring wedges are tied together through the C-terminal dimer of gp6. The dimeric interactions are preserved throughout the rearrangement of the baseplate. However, the hinge angle between the N- and C-terminal parts of gp6 changes by approximately 15 degrees , accounting for a 10 A radial increase in the diameter of the gp6 ring.
-The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate.,Aksyuk AA, Leiman PG, Shneider MM, Mesyanzhinov VV, Rossmann MG Structure. 2009 Jun 10;17(6):800-8. PMID:19523898<ref>PMID:19523898</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3h2t" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bpt4]]
+[[Category: Escherichia virus T4]]
-[[Category: Aksyuk, A A]]
+[[Category: Large Structures]]
-[[Category: Leiman, P G]]
+[[Category: Aksyuk AA]]
-[[Category: Mesyanzhinov, V V]]
+[[Category: Leiman PG]]
-[[Category: Rossmann, M G]]
+[[Category: Mesyanzhinov VV]]
-[[Category: Shneider, M M]]
+[[Category: Rossmann MG]]
-[[Category: Viral protein]]
+[[Category: Shneider MM]]
-[[Category: Virion]]