2mjz

<StructureSection load='2mjz' size='340' side='right'caption='[[2mjz]], [[NMR_Ensembles_of_Models | 3 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2mjz]] is a 35 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MJZ 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=2mjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mjz OCA], [https://pdbe.org/2mjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mjz RCSB], [https://www.ebi.ac.uk/pdbsum/2mjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mjz ProSAT]</span></td></tr>

[[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.

Filamentous phage are elongated semiflexible ssDNA viruses that infect bacteria. The M13 phage, belonging to the family inoviridae, has a length of approximately 1 mum and a diameter of approximately 7 nm. Here we present a structural model for the capsid of intact M13 bacteriophage using Rosetta model building guided by structure restraints obtained from magic-angle spinning solid-state NMR experimental data. The C5 subunit symmetry observed in fiber diffraction studies was enforced during model building. The structure consists of stacked pentamers with largely alpha helical subunits containing an N-terminal type II beta-turn; there is a rise of 16.6-16.7 A and a tilt of 36.1-36.6 degrees between consecutive pentamers. The packing of the subunits is stabilized by a repeating hydrophobic stacking pocket; each subunit participates in four pockets by contributing different hydrophobic residues, which are spread along the subunit sequence. Our study provides, to our knowledge, the first magic-angle spinning NMR structure of an intact filamentous virus capsid and further demonstrates the strength of this technique as a method of choice to study noncrystalline, high-molecular-weight molecular assemblies.

 

== References ==

[[Category: Baker, D]]

[[Category: Goldbourt, A]]

[[Category: Morag, O]]

[[Category: Sgourakis, N G]]

[[Category: Viral protein]]