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==P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links==
==P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links==
<StructureSection load='3iyh' size='340' side='right' caption='[[3iyh]], [[Resolution|resolution]] 8.20&Aring;' scene=''>
<SX load='3iyh' size='340' side='right' viewer='molstar' caption='[[3iyh]], [[Resolution|resolution]] 8.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3iyh]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IYH FirstGlance]. <br>
<table><tr><td colspan='2'>[[3iyh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IYH FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3iyi|3iyi]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.2&#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=3iyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iyh OCA], [http://pdbe.org/3iyh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3iyh RCSB], [http://www.ebi.ac.uk/pdbsum/3iyh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3iyh 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=3iyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iyh OCA], [https://pdbe.org/3iyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iyh RCSB], [https://www.ebi.ac.uk/pdbsum/3iyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iyh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VG05_BPP22 VG05_BPP22]] Required for successful condensation of DNA within the capsid. Gp5 is the major structural protein of the outer shell of the prohead.  
[https://www.uniprot.org/uniprot/CAPSD_BPP22 CAPSD_BPP22] Assembles to form an icosahedral capsid with a T=7 symmetry.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/3iyh_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/3iyh_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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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=3iyh 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=3iyh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Viral capsid assembly and stability in tailed, dsDNA phage and Herpesviridae are achieved by various means including chemical crosslinks (unique to HK97), or auxiliary proteins (lambda, T4, phi29, and herpesviruses). All these viruses have coat proteins (CP) with a conserved, HK97-like core structure. We used a combination of trypsin digestion, gold labeling, cryo-electron microscopy, 3D image reconstruction, and comparative modeling to derive two independent, pseudoatomic models of bacteriophage P22 CP: before and after maturation. P22 capsid stabilization results from intersubunit interactions among N-terminal helices and an extensive "P loop," which obviate the need for crosslinks or auxiliary proteins. P22 CP also has a telokin-like Ig domain that likely stabilizes the monomer fold so that assembly may proceed via individual subunit addition rather than via preformed capsomers as occurs in HK97. Hence, the P22 CP structure may be a paradigm for understanding how monomers assemble in viruses like phi29 and HSV-1.
P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks.,Parent KN, Khayat R, Tu LH, Suhanovsky MM, Cortines JR, Teschke CM, Johnson JE, Baker TS Structure. 2010 Mar 10;18(3):390-401. PMID:20223221<ref>PMID:20223221</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3iyh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Enterobacteria phage p22]]
[[Category: Large Structures]]
[[Category: Baker, T S]]
[[Category: Salmonella virus P22]]
[[Category: Cortines, J R]]
[[Category: Baker TS]]
[[Category: Johnson, J E]]
[[Category: Cortines JR]]
[[Category: Khayat, R]]
[[Category: Johnson JE]]
[[Category: Parent, K N]]
[[Category: Khayat R]]
[[Category: Suhanovsky, M M]]
[[Category: Parent KN]]
[[Category: Teschke, C M]]
[[Category: Suhanovsky MM]]
[[Category: Tu, L H]]
[[Category: Teschke CM]]
[[Category: Capsid protein]]
[[Category: Tu LH]]
[[Category: Hk97-like fold]]
[[Category: Late protein]]
[[Category: Virion]]
[[Category: Virus]]

Latest revision as of 13:07, 21 February 2024

P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-linksP22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links

3iyh, resolution 8.20Å

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OCA
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