View source for 1gw8


==quasi-atomic resolution model of bacteriophage PRD1 sus607 mutant, obtained by combined cryo-EM and X-ray crystallography.==
<SX load='1gw8' size='340' side='right' viewer='molstar' caption='[[1gw8]], [[Resolution|resolution]] 13.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gw8]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_PRD1 Enterobacteria phage PRD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GW8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GW8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 13.3&#8491;</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=1gw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gw8 OCA], [https://pdbe.org/1gw8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gw8 RCSB], [https://www.ebi.ac.uk/pdbsum/1gw8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gw8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAPSD_BPPRD CAPSD_BPPRD] Major capsid protein self-assembles to form an icosahedral capsid with a pseudo T=25 symmetry, about 66 nm in diameter, and consisting of 240 capsid proteins trimers. The capsid encapsulates an inner membrane and the genomic dsDNA genome. The major coat protein P3 and two assembly factors (P10 and P17) are needed during the assembly of the virus particle inside the host cell, when the capsid protein multimers are capable of enclosing the host-derived membrane, containing the virus-encoded membrane-associated proteins.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteriophage PRD1 shares many structural and functional similarities with adenovirus. A major difference is the PRD1 internal membrane, which acts in concert with vertex proteins to translocate the phage genome into the host. Multiresolution models of the PRD1 capsid, together with genetic analyses, provide fine details of the molecular interactions associated with particle stability and membrane dynamics. The N- and C-termini of the major coat protein (P3), which are required for capsid assembly, act as conformational switches bridging capsid to membrane and linking P3 trimers. Electrostatic P3-membrane interactions increase virion stability upon DNA packaging. Newly revealed proteins suggest how the metastable vertex works and how the capsid edges are stabilized.

Minor proteins, mobile arms and membrane-capsid interactions in the bacteriophage PRD1 capsid.,San Martin C, Huiskonen JT, Bamford JK, Butcher SJ, Fuller SD, Bamford DH, Burnett RM Nat Struct Biol. 2002 Oct;9(10):756-63. PMID:12219080<ref>PMID:12219080</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1gw8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Enterobacteria phage PRD1]]
[[Category: Large Structures]]
[[Category: Bamford DH]]
[[Category: Bamford JKH]]
[[Category: Burnett RM]]
[[Category: Butcher SJ]]
[[Category: Fuller SD]]
[[Category: Huiskonen J]]
[[Category: San Martin C]]