4blo: Difference between revisions
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==P4 PROTEIN FROM BACTERIOPHAGE PHI6 IN COMPLEX WITH ADP== | ==P4 PROTEIN FROM BACTERIOPHAGE PHI6 IN COMPLEX WITH ADP== | ||
<StructureSection load='4blo' size='340' side='right' caption='[[4blo]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='4blo' size='340' side='right'caption='[[4blo]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4blo]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4blo]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_phi6 Pseudomonas virus phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BLO FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4blo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4blo OCA], [https://pdbe.org/4blo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4blo RCSB], [https://www.ebi.ac.uk/pdbsum/4blo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4blo ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/P4_BPPH6 P4_BPPH6] P4 is one of the structural proteins of the polyhedral procapsid, which is responsible for genomic replication and transcription. Displays single-stranded RNA-stimulated NTPase activity.<ref>PMID:12239286</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 24: | Line 23: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas virus phi6]] | ||
[[Category: Bamford | [[Category: Bamford DH]] | ||
[[Category: | [[Category: El Omari K]] | ||
[[Category: | [[Category: Grimes JM]] | ||
[[Category: | [[Category: Kainov D]] | ||
[[Category: | [[Category: Mancini EJ]] | ||
[[Category: | [[Category: Meier C]] | ||
[[Category: Poranen | [[Category: Poranen MM]] | ||
[[Category: Stuart | [[Category: Stuart DI]] | ||
[[Category: Sutton | [[Category: Sutton G]] | ||
[[Category: Tuma | [[Category: Tuma R]] | ||
Latest revision as of 14:02, 9 May 2024
P4 PROTEIN FROM BACTERIOPHAGE PHI6 IN COMPLEX WITH ADPP4 PROTEIN FROM BACTERIOPHAGE PHI6 IN COMPLEX WITH ADP
Structural highlights
FunctionP4_BPPH6 P4 is one of the structural proteins of the polyhedral procapsid, which is responsible for genomic replication and transcription. Displays single-stranded RNA-stimulated NTPase activity.[1] Publication Abstract from PubMedMany 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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