2m5s
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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 == | ||
[https://www.uniprot.org/uniprot/CAPSD_BPP22 CAPSD_BPP22] Assembles to form an icosahedral capsid with a T=7 symmetry. | [https://www.uniprot.org/uniprot/CAPSD_BPP22 CAPSD_BPP22] Assembles to form an icosahedral capsid with a T=7 symmetry. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
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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