2m5s

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==High-resolution NMR structure and cryo-EM imaging support multiple functional roles for the accessory I-domain of phage P22 coat protein==
==High-resolution NMR structure and cryo-EM imaging support multiple functional roles for the accessory I-domain of phage P22 coat protein==
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<StructureSection load='2m5s' size='340' side='right'caption='[[2m5s]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
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<StructureSection load='2m5s' size='340' side='right'caption='[[2m5s]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2m5s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M5S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2m5s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M5S FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3iyi|3iyi]], [[3iyh|3iyh]], [[2xyy|2xyy]], [[2xyz|2xyz]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5, gp5 coat protein ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10754 BPP22])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m5s OCA], [https://pdbe.org/2m5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m5s RCSB], [https://www.ebi.ac.uk/pdbsum/2m5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m5s 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=2m5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m5s OCA], [https://pdbe.org/2m5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m5s RCSB], [https://www.ebi.ac.uk/pdbsum/2m5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m5s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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.
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[https://www.uniprot.org/uniprot/CAPSD_BPP22 CAPSD_BPP22] Assembles to form an icosahedral capsid with a T=7 symmetry.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique insertion domain (I-domain). Two prior I-domain models from subnanometer cryoelectron microscopy (cryoEM) reconstructions differed substantially. Therefore, the I-domain's nuclear magnetic resonance structure was determined and also used to improve cryoEM models of coat protein. The I-domain has an antiparallel six-stranded beta-barrel fold, not previously observed in HK97-fold accessory domains. The D-loop, which is dynamic in the isolated I-domain and intact monomeric coat protein, forms stabilizing salt bridges between adjacent capsomers in procapsids. The S-loop is important for capsid size determination, likely through intrasubunit interactions. Ten of 18 coat protein temperature-sensitive-folding substitutions are in the I-domain, indicating its importance in folding and stability. Several are found on a positively charged face of the beta-barrel that anchors the I-domain to a negatively charged surface of the coat protein HK97-core.
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Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.,Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM Structure. 2014 Jun 10;22(6):830-41. doi: 10.1016/j.str.2014.04.003. Epub 2014, May 15. PMID:24836025<ref>PMID:24836025</ref>
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2m5s" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bpp22]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Alexandrescu, A T]]
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[[Category: Salmonella virus P22]]
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[[Category: Baker, M L]]
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[[Category: Alexandrescu AT]]
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[[Category: Chiu, W]]
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[[Category: Baker ML]]
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[[Category: Fraser, L C.R]]
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[[Category: Chiu W]]
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[[Category: Gross, M L]]
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[[Category: Fraser LCR]]
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[[Category: Jones, L M]]
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[[Category: Gross ML]]
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[[Category: Rempel, D L]]
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[[Category: Jones LM]]
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[[Category: Rizzo, A A]]
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[[Category: Rempel DL]]
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[[Category: Suhanovsky, M M]]
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[[Category: Rizzo AA]]
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[[Category: Teschke, C M]]
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[[Category: Suhanovsky MM]]
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[[Category: D-loop]]
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[[Category: Teschke CM]]
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[[Category: Extra-density domain]]
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[[Category: Telokin-like domain]]
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[[Category: Viral protein]]
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Current revision

High-resolution NMR structure and cryo-EM imaging support multiple functional roles for the accessory I-domain of phage P22 coat protein

PDB ID 2m5s

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