2cpb: Difference between revisions
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< | ==SOLUTION NMR STRUCTURES OF THE MAJOR COAT PROTEIN OF FILAMENTOUS BACTERIOPHAGE M13 SOLUBILIZED IN DODECYLPHOSPHOCHOLINE MICELLES, 25 LOWEST ENERGY STRUCTURES== | ||
<StructureSection load='2cpb' size='340' side='right'caption='[[2cpb]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2cpb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_M13 Escherichia virus M13]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CPB 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=2cpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cpb OCA], [https://pdbe.org/2cpb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cpb RCSB], [https://www.ebi.ac.uk/pdbsum/2cpb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cpb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAPSD_BPM13 CAPSD_BPM13] 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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The three-dimensional structure of the major coat protein of bacteriophage M13, solubilized in detergent micelles, has been determined using heteronuclear multidimensional NMR and restrained molecular dynamics. The protein consists of two alpha-helices, running from residues 8 to 16 and 25 to 45, respectively. These two helices are connected by a flexible and distorted helical hinge region. The structural properties of the coat protein make it resemble a flail, in which the hydrophobic helix (residues 25 to 45) is the handle and the other, amphipathic, helix the swingle. In this metaphor, the hinge region is the connecting piece of leather. The mobility of the residues in the hinge region is likely to enable a smooth transformation from the membrane-bound form, mimicked by the structure in detergent micelles, into the structure in the mature phage. A specific distribution of the residues over the surface of the two helices was observed in the presented high-resolution structure of the membrane-bound form of the major coat protein as well as in the structure in the mature phage. All data suggest that this arrangement of residues is important for the interactions of the protein with the membrane, for correct protein-DNA and protein-protein interactions in the phage and for a proper growth of the phage during the assembly process. By combining our findings with earlier NMR results on the major coat protein in detergent micelles, we were able to construct a model that addresses the role of specific residues in the assembly process. | |||
Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues.,Papavoine CH, Christiaans BE, Folmer RH, Konings RN, Hilbers CW J Mol Biol. 1998 Sep 18;282(2):401-19. PMID:9735296<ref>PMID:9735296</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2cpb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Escherichia virus M13]] | ||
[[Category: Large Structures]] | |||
[[Category: Christiaans BEC]] | |||
== | [[Category: Folmer RHA]] | ||
[[Category: Hilbers CW]] | |||
[[Category: | [[Category: Konings RNH]] | ||
[[Category: | [[Category: Papavoine CHM]] | ||
[[Category: Christiaans | |||
[[Category: Folmer | |||
[[Category: Hilbers | |||
[[Category: Konings | |||
[[Category: Papavoine | |||
Latest revision as of 12:24, 22 May 2024
SOLUTION NMR STRUCTURES OF THE MAJOR COAT PROTEIN OF FILAMENTOUS BACTERIOPHAGE M13 SOLUBILIZED IN DODECYLPHOSPHOCHOLINE MICELLES, 25 LOWEST ENERGY STRUCTURESSOLUTION NMR STRUCTURES OF THE MAJOR COAT PROTEIN OF FILAMENTOUS BACTERIOPHAGE M13 SOLUBILIZED IN DODECYLPHOSPHOCHOLINE MICELLES, 25 LOWEST ENERGY STRUCTURES
Structural highlights
FunctionCAPSD_BPM13 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. Publication Abstract from PubMedThe three-dimensional structure of the major coat protein of bacteriophage M13, solubilized in detergent micelles, has been determined using heteronuclear multidimensional NMR and restrained molecular dynamics. The protein consists of two alpha-helices, running from residues 8 to 16 and 25 to 45, respectively. These two helices are connected by a flexible and distorted helical hinge region. The structural properties of the coat protein make it resemble a flail, in which the hydrophobic helix (residues 25 to 45) is the handle and the other, amphipathic, helix the swingle. In this metaphor, the hinge region is the connecting piece of leather. The mobility of the residues in the hinge region is likely to enable a smooth transformation from the membrane-bound form, mimicked by the structure in detergent micelles, into the structure in the mature phage. A specific distribution of the residues over the surface of the two helices was observed in the presented high-resolution structure of the membrane-bound form of the major coat protein as well as in the structure in the mature phage. All data suggest that this arrangement of residues is important for the interactions of the protein with the membrane, for correct protein-DNA and protein-protein interactions in the phage and for a proper growth of the phage during the assembly process. By combining our findings with earlier NMR results on the major coat protein in detergent micelles, we were able to construct a model that addresses the role of specific residues in the assembly process. Solution structure of the M13 major coat protein in detergent micelles: a basis for a model of phage assembly involving specific residues.,Papavoine CH, Christiaans BE, Folmer RH, Konings RN, Hilbers CW J Mol Biol. 1998 Sep 18;282(2):401-19. PMID:9735296[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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