3ddx
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<SX load='3ddx' size='340' side='right' viewer='molstar' caption='[[3ddx]]' scene=''> | <SX load='3ddx' size='340' side='right' viewer='molstar' caption='[[3ddx]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3ddx]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3ddx]] 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=3DDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DDX FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ddx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ddx OCA], [https://pdbe.org/3ddx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ddx RCSB], [https://www.ebi.ac.uk/pdbsum/3ddx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ddx 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=3ddx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ddx OCA], [https://pdbe.org/3ddx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ddx RCSB], [https://www.ebi.ac.uk/pdbsum/3ddx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ddx ProSAT]</span></td></tr> | ||
</table> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[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=3ddx ConSurf]. | </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=3ddx ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The capsids of tailed-DNA bacteriophages first assemble as procapsids, which mature by converting into a new form that is strong enough to contain a densely packed viral chromosome. We demonstrate that the intersubunit crosslinking that occurs during maturation of HK97 capsids actually promotes the structural transformation. Small-angle X-ray scattering and crosslinking assays reveal that a shift in the crosslink pattern accompanies conversion of a semimature particle, Expansion Intermediate-I/II, to a more mature state, Balloon. This transition occurs in a switch-like fashion. We find that crosslink formation shifts the global conformational balance to favor the balloon state. A pseudoatomic model of EI-I/II derived from cryo-EM provides insight into the relationship between crosslink formation and conformational switching. | ||
| - | |||
| - | Virus capsid expansion driven by the capture of mobile surface loops.,Lee KK, Gan L, Tsuruta H, Moyer C, Conway JF, Duda RL, Hendrix RW, Steven AC, Johnson JE Structure. 2008 Oct 8;16(10):1491-502. PMID:18940605<ref>PMID:18940605</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3ddx" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
| - | [[Category: | + | [[Category: Escherichia virus HK97]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Conway | + | [[Category: Conway JF]] |
| - | [[Category: Gan | + | [[Category: Gan L]] |
| - | [[Category: Hendrix | + | [[Category: Hendrix RW]] |
| - | [[Category: Johnson | + | [[Category: Johnson JE]] |
| - | [[Category: Lee | + | [[Category: Lee KK]] |
| - | [[Category: Steven | + | [[Category: Steven AC]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Revision as of 09:40, 21 February 2024
HK97 bacteriophage capsid Expansion Intermediate-II model
| |||||||||
