View source for 5ft1


==Crystal structure of gp37(Dip) from bacteriophage phiKZ bound to RNase E of Pseudomonas aeruginosa==
<StructureSection load='5ft1' size='340' side='right'caption='[[5ft1]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ft1]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] and [https://en.wikipedia.org/wiki/Pseudomonas_virus_phiKZ Pseudomonas virus phiKZ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FT1 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]] 2.75&#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=5ft1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ft1 OCA], [https://pdbe.org/5ft1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ft1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ft1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ft1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8SDC5_BPDPK Q8SDC5_BPDPK] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In all domains of life, the catalysed degradation of RNA facilitates rapid adaptation to changing environmental conditions, while destruction of foreign RNA is an important mechanism to prevent host infection. We have identified a virus-encoded protein termed gp37/Dip, which directly binds and inhibits the RNA degradation machinery of its bacterial host. Encoded by giant phage PhiKZ, this protein associates with two RNA binding sites of the RNase E component of the Pseudomonas aeruginosa RNA degradosome, occluding them from substrates and resulting in effective inhibition of RNA degradation and processing. The 2.2 A crystal structure reveals that this novel homo-dimeric protein has no identifiable structural homologues. Our biochemical data indicate that acidic patches on the convex outer surface bind RNase E. Through the activity of Dip, PhiKZ has evolved a unique mechanism to down regulate a key metabolic process of its host to allow accumulation of viral RNA in infected cells.

Structural elucidation of a novel mechanism for the bacteriophage-based inhibition of the RNA degradosome.,Van den Bossche A, Hardwick SW, Ceyssens PJ, Hendrix H, Voet M, Dendooven T, Bandyra KJ, De Maeyer M, Aertsen A, Noben JP, Luisi BF, Lavigne R Elife. 2016 Jul 22;5. pii: e16413. doi: 10.7554/eLife.16413. PMID:27447594<ref>PMID:27447594</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ft1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas virus phiKZ]]
[[Category: Aertsen A]]
[[Category: Bandyra KJ]]
[[Category: Ceyssens PJ]]
[[Category: De Maeyer M]]
[[Category: Dendooven T]]
[[Category: Hardwick SW]]
[[Category: Hendrix H]]
[[Category: Lavigne R]]
[[Category: Luisi BF]]
[[Category: Noben JP]]
[[Category: Van den Bossche A]]
[[Category: Voet M]]