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==Membrane-bound structure of the Pf1 major coat protein in DHPC micelle== | |||
<StructureSection load='2klv' size='340' side='right'caption='[[2klv]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2klv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_Pf1 Pseudomonas virus Pf1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KLV FirstGlance]. <br> | |||
</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=2klv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klv OCA], [https://pdbe.org/2klv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2klv RCSB], [https://www.ebi.ac.uk/pdbsum/2klv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2klv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAPSD_BPPF1 CAPSD_BPPF1] Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
At pH > 6 added filamentous bacteriophage fd is compatible with many of the detergents used to solubilize membrane proteins for solution NMR studies of membrane proteins and, therefore, serves as an alignment media. In combination with strained polyacrylamide gel alignment, Dipolar Waves can be used to directly assess the secondary structure and a lambda-map extracts the order tensors for de novo structure calculation of membrane proteins without distance restraints. | |||
Phage-Induced Alignment of Membrane Proteins Enables the Measurement and Structural Analysis of Residual Dipolar Couplings with Dipolar Waves and lambda-Maps.,Park SH, Son WS, Mukhopadhyay R, Valafar H, Opella SJ J Am Chem Soc. 2009 Sep 17. PMID:19761238<ref>PMID:19761238</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2klv" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: Pseudomonas | </StructureSection> | ||
[[Category: Mukhopadhyay | [[Category: Large Structures]] | ||
[[Category: Opella | [[Category: Pseudomonas virus Pf1]] | ||
[[Category: Park | [[Category: Mukhopadhyay R]] | ||
[[Category: Son | [[Category: Opella SJ]] | ||
[[Category: Valafar | [[Category: Park S]] | ||
[[Category: Son W]] | |||
[[Category: Valafar H]] | |||
Latest revision as of 12:40, 22 May 2024
Membrane-bound structure of the Pf1 major coat protein in DHPC micelleMembrane-bound structure of the Pf1 major coat protein in DHPC micelle
Structural highlights
FunctionCAPSD_BPPF1 Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity). Publication Abstract from PubMedAt pH > 6 added filamentous bacteriophage fd is compatible with many of the detergents used to solubilize membrane proteins for solution NMR studies of membrane proteins and, therefore, serves as an alignment media. In combination with strained polyacrylamide gel alignment, Dipolar Waves can be used to directly assess the secondary structure and a lambda-map extracts the order tensors for de novo structure calculation of membrane proteins without distance restraints. Phage-Induced Alignment of Membrane Proteins Enables the Measurement and Structural Analysis of Residual Dipolar Couplings with Dipolar Waves and lambda-Maps.,Park SH, Son WS, Mukhopadhyay R, Valafar H, Opella SJ J Am Chem Soc. 2009 Sep 17. PMID:19761238[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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