3ig9: Difference between revisions

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 <StructureSection load='3ig9' size='340' side='right'caption='[[3ig9]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ig9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpr69 Bpr69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IG9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ig9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_RB69 Escherichia phage RB69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IG9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IG9 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ige|3ige]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">soc ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=12353 BPR69])</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=3ig9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ig9 OCA], [https://pdbe.org/3ig9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ig9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ig9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ig9 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SOC_BPR69 SOC_BPR69] Capsid decoration protein which helps to stabilize the capsid against extremes of pH and temperature. Once maturation and expansion of the capsid has occured, trimers of soc attach the interfaces between the hexamer of the major capsid protein. Acts as a 'glue' between neighboring hexameric capsomers. Dispensable for the head morphogenesis and phage infection.[HAMAP-Rule:MF_04115]
 == 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=3ig9 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Many viruses need to stabilize their capsid structure against DNA pressure and for survival in hostile environments. The 9-kDa outer capsid protein (Soc) of bacteriophage T4, which stabilizes the virus, attaches to the capsid during the final stage of maturation. There are 870 Soc molecules that act as a "glue" between neighboring hexameric capsomers, forming a "cage" that stabilizes the T4 capsid against extremes of pH and temperature. Here we report a 1.9 A resolution crystal structure of Soc from the bacteriophage RB69, a close relative of T4. The RB69 crystal structure and a homology model of T4 Soc were fitted into the cryoelectron microscopy reconstruction of the T4 capsid. This established the region of Soc that interacts with the major capsid protein and suggested a mechanism, verified by extensive mutational and biochemical studies, for stabilization of the capsid in which the Soc trimers act as clamps between neighboring capsomers. The results demonstrate the factors involved in stabilizing not only the capsids of T4-like bacteriophages but also many other virus capsids.
-Structure of the small outer capsid protein, Soc: a clamp for stabilizing capsids of T4-like phages.,Qin L, Fokine A, O'Donnell E, Rao VB, Rossmann MG J Mol Biol. 2010 Jan 29;395(4):728-41. Epub 2009 Oct 14. PMID:19835886<ref>PMID:19835886</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3ig9" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bpr69]]
+[[Category: Escherichia phage RB69]]
 [[Category: Large Structures]]
-[[Category: Donnell, E O]]
+[[Category: Fokine A]]
-[[Category: Fokine, A]]
+[[Category: Li Q]]
-[[Category: Li, Q]]
+[[Category: O'Donnell E]]
-[[Category: Rao, V B]]
+[[Category: Rao VB]]
-[[Category: Rossmann, M G]]
+[[Category: Rossmann MG]]
-[[Category: Alpha/beta structure]]
-[[Category: Viral protein]]