View source for 3qhs


==Crystal structure of full-length Hfq from Escherichia coli==
<StructureSection load='3qhs' size='340' side='right'caption='[[3qhs]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qhs]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QHS 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]] 2.85&#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=3qhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhs OCA], [https://pdbe.org/3qhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qhs RCSB], [https://www.ebi.ac.uk/pdbsum/3qhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qhs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HFQ_ECOLI HFQ_ECOLI] RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Involved in the regulation of stress responses mediated by the sigma factors RpoS, sigma-E and sigma-32. Binds with high specificity to tRNAs. In vitro, stimulates synthesis of long tails by poly(A) polymerase I. Required for RNA phage Qbeta replication.<ref>PMID:805130</ref> <ref>PMID:10677490</ref> <ref>PMID:11222598</ref> <ref>PMID:17158661</ref> <ref>PMID:19909729</ref>   Seems to play a role in persister cell formation; upon overexpression decreases persister cell formation while deletion increases persister formation.<ref>PMID:805130</ref> <ref>PMID:10677490</ref> <ref>PMID:11222598</ref> <ref>PMID:17158661</ref> <ref>PMID:19909729</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of full-length host factor Qbeta (Hfq) from Escherichia coli obtained from a crystal belonging to space group P1, with unit-cell parameters a = 61.91, b = 62.15, c = 81.26 A, alpha = 78.6, beta = 86.2, gamma = 59.9 degrees , was solved by molecular replacement to a resolution of 2.85 A and refined to R(work) and R(free) values of 20.7% and 25.0%, respectively. Hfq from E. coli has previously been crystallized and the structure has been solved for the N-terminal 72 amino acids, which cover approximately 65% of the full-length sequence. Here, the purification, crystallization and structural data of the full 102-amino-acid protein are presented. These data revealed that the presence of the C-terminus changes the crystal packing of E. coli Hfq. The crystal structure is discussed in the context of the recently published solution structure of Hfq from E. coli.

Structural analysis of full-length Hfq from Escherichia coli.,Beich-Frandsen M, Vecerek B, Sjoblom B, Blasi U, Djinovic-Carugo K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):536-40. Epub 2011 Apr 20. PMID:21543856<ref>PMID:21543856</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qhs" style="background-color:#fffaf0;"></div>

==See Also==
*[[Protein Hfq 3D structures|Protein Hfq 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Beich-Frandsen M]]
[[Category: Blaesi U]]
[[Category: Djinovic-Carugo K]]
[[Category: Sjoeblom B]]
[[Category: Vecerek B]]