2fte: Difference between revisions

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 <SX load='2fte' size='340' side='right' viewer='molstar' caption='[[2fte]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2fte]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bphk7 Bphk7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FTE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2fte]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_HK97 Escherichia virus HK97]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FTE FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2frp|2frp]], [[2fs3|2fs3]], [[2fsy|2fsy]], [[2ft1|2ft1]], [[1ohg|1ohg]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37554 BPHK7])</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=2fte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fte OCA], [https://pdbe.org/2fte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fte RCSB], [https://www.ebi.ac.uk/pdbsum/2fte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fte ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CAPSD_BPHK7 CAPSD_BPHK7] Assembles to form an icosahedral capsid of 66 nm, with a T=7 laevo symmetry (PubMed:11000116, PubMed:21276801). Responsible for its self-assembly into a procapsid. The phage does not need to encode a separate scaffolfing protein because its capsid protein contains the delta domain that carries that function.<ref>PMID:11000116</ref> <ref>PMID:21276801</ref> <ref>PMID:7669350</ref> <ref>PMID:7723020</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 18: / 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=2fte ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Maturation of the bacteriophage HK97 capsid from a precursor (Prohead II) to the mature state (Head II) involves a 60 A radial expansion. The mature particle is formed by 420 copies of the major capsid protein organized on a T = 7 laevo lattice with each subunit covalently crosslinked to two neighbors. Well-characterized pH 4 expansion intermediates make HK97 valuable for investigating quaternary structural dynamics. Here, we use X-ray crystallography and cryo-EM to demonstrate that in the final transition in maturation (requiring neutral pH), pentons in Expansion Intermediate IV (EI-IV) reversibly sample 14 A translations and 6 degrees rotations relative to a fixed hexon lattice. The limit of this trajectory corresponds to the Head II conformation that is secured at this extent only by the formation of the final class of covalent crosslinks. Mutants that cannot crosslink or EI-IV particles that have been rendered incapable of forming the final crosslink remain in the EI-IV state.
-Capsid conformational sampling in HK97 maturation visualized by X-ray crystallography and cryo-EM.,Gan L, Speir JA, Conway JF, Lander G, Cheng N, Firek BA, Hendrix RW, Duda RL, Liljas L, Johnson JE Structure. 2006 Nov;14(11):1655-65. PMID:17098191<ref>PMID:17098191</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2fte" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </SX>
-[[Category: Bphk7]]
+[[Category: Escherichia virus HK97]]
 [[Category: Large Structures]]
-[[Category: Cheng, N]]
+[[Category: Cheng N]]
-[[Category: Conway, J F]]
+[[Category: Conway JF]]
-[[Category: Duda, R L]]
+[[Category: Duda RL]]
-[[Category: Firek, B A]]
+[[Category: Firek BA]]
-[[Category: Gan, L]]
+[[Category: Gan L]]
-[[Category: Hendrix, R W]]
+[[Category: Hendrix RW]]
-[[Category: Johnson, J E]]
+[[Category: Johnson JE]]
-[[Category: Lander, G]]
+[[Category: Lander G]]
-[[Category: Liljas, L]]
+[[Category: Liljas L]]
-[[Category: Speir, J A]]
+[[Category: Speir JA]]
-[[Category: Bacteriophage]]
-[[Category: Capsid protein]]
-[[Category: Expansion intermediate]]
-[[Category: Hk97]]
-[[Category: Virus-viral protein complex]]