View source for 4bwy


==P4 PROTEIN FROM BACTERIOPHAGE PHI8 (R32)==
<StructureSection load='4bwy' size='340' side='right'caption='[[4bwy]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bwy]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_phi8 Pseudomonas phage phi8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BWY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#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=4bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwy OCA], [https://pdbe.org/4bwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bwy RCSB], [https://www.ebi.ac.uk/pdbsum/4bwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bwy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9MC14_9VIRU Q9MC14_9VIRU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many complex viruses package their genomes into empty protein shells and bacteriophages of the Cystoviridae family provide some of the simplest models for this. The cystoviral hexameric NTPase, P4, uses chemical energy to translocate single-stranded RNA genomic precursors into the procapsid. We previously dissected the mechanism of RNA translocation for one such phage, 12, and have now investigated three further highly divergent, cystoviral P4 NTPases (from 6, 8 and 13). High-resolution crystal structures of the set of P4s allow a structure-based phylogenetic analysis, which reveals that these proteins form a distinct subfamily of the RecA-type ATPases. Although the proteins share a common catalytic core, they have different specificities and control mechanisms, which we map onto divergent N- and C-terminal domains. Thus, the RNA loading and tight coupling of NTPase activity with RNA translocation in 8 P4 is due to a remarkable C-terminal structure, which wraps right around the outside of the molecule to insert into the central hole where RNA binds to coupled L1 and L2 loops, whereas in 12 P4, a C-terminal residue, serine 282, forms a specific hydrogen bond to the N7 of purines ring to confer purine specificity for the 12 enzyme.

Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution.,El Omari K, Meier C, Kainov D, Sutton G, Grimes JM, Poranen MM, Bamford DH, Tuma R, Stuart DI, Mancini EJ Nucleic Acids Res. 2013 Aug 11. PMID:23939620<ref>PMID:23939620</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bwy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas phage phi8]]
[[Category: Bamford DH]]
[[Category: El Omari K]]
[[Category: Grimes JM]]
[[Category: Kainov D]]
[[Category: Mancini EJ]]
[[Category: Meier C]]
[[Category: Poranen MM]]
[[Category: Stuart DI]]
[[Category: Sutton G]]
[[Category: Tuma R]]