2klv: Difference between revisions

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==Membrane-bound structure of the Pf1 major coat protein in DHPC micelle==
==Membrane-bound structure of the Pf1 major coat protein in DHPC micelle==
<StructureSection load='2klv' size='340' side='right' caption='[[2klv]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
<StructureSection load='2klv' size='340' side='right'caption='[[2klv]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2klv]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KLV FirstGlance]. <br>
<table><tr><td colspan='2'>[[2klv]] is a 1 chain structure. 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 [http://proteopedia.org/fgij/fg.htm?mol=2KLV FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pjf|1pjf]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pjf|1pjf]]</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=2klv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klv OCA], [http://pdbe.org/2klv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2klv RCSB], [http://www.ebi.ac.uk/pdbsum/2klv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2klv ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2klv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klv OCA], [http://pdbe.org/2klv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2klv RCSB], [http://www.ebi.ac.uk/pdbsum/2klv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2klv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Mukhopadhyay, R]]
[[Category: Mukhopadhyay, R]]
[[Category: Opella, S J]]
[[Category: Opella, S J]]

Revision as of 10:33, 29 April 2020

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

2klv is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Park SH, Son WS, Mukhopadhyay R, Valafar H, Opella SJ. Phage-Induced Alignment of Membrane Proteins Enables the Measurement and Structural Analysis of Residual Dipolar Couplings with Dipolar Waves and lambda-Maps. J Am Chem Soc. 2009 Sep 17. PMID:19761238 doi:10.1021/ja905640d
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