3qhs

From Proteopedia

(Difference between revisions)

Revision as of 06:09, 8 June 2022

Crystal structure of full-length Hfq from Escherichia coli

Structural highlights

3qhs is a 12 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3qo3
Gene:	b4172, hfq, JW4130 (ECOLI)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] ^[4] ^[5] Seems to play a role in persister cell formation; upon overexpression decreases persister cell formation while deletion increases persister formation.^[6] ^[7] ^[8] ^[9] ^[10]

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^[11]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Carmichael GG, Weber K, Niveleau A, Wahba AJ. The host factor required for RNA phage Qbeta RNA replication in vitro. Intracellular location, quantitation, and purification by polyadenylate-cellulose chromatography. J Biol Chem. 1975 May 25;250(10):3607-612. PMID:805130
↑ Hajnsdorf E, Regnier P. Host factor Hfq of Escherichia coli stimulates elongation of poly(A) tails by poly(A) polymerase I. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1501-5. PMID:10677490 doi:10.1073/pnas.040549897
↑ Sledjeski DD, Whitman C, Zhang A. Hfq is necessary for regulation by the untranslated RNA DsrA. J Bacteriol. 2001 Mar;183(6):1997-2005. PMID:11222598 doi:10.1128/JB.183.6.1997-2005.2001
↑ Guisbert E, Rhodius VA, Ahuja N, Witkin E, Gross CA. Hfq modulates the sigmaE-mediated envelope stress response and the sigma32-mediated cytoplasmic stress response in Escherichia coli. J Bacteriol. 2007 Mar;189(5):1963-73. Epub 2006 Dec 8. PMID:17158661 doi:10.1128/JB.01243-06
↑ Kim Y, Wood TK. Toxins Hha and CspD and small RNA regulator Hfq are involved in persister cell formation through MqsR in Escherichia coli. Biochem Biophys Res Commun. 2010 Jan 1;391(1):209-13. doi:, 10.1016/j.bbrc.2009.11.033. Epub 2009 Nov 10. PMID:19909729 doi:10.1016/j.bbrc.2009.11.033
↑ Carmichael GG, Weber K, Niveleau A, Wahba AJ. The host factor required for RNA phage Qbeta RNA replication in vitro. Intracellular location, quantitation, and purification by polyadenylate-cellulose chromatography. J Biol Chem. 1975 May 25;250(10):3607-612. PMID:805130
↑ Hajnsdorf E, Regnier P. Host factor Hfq of Escherichia coli stimulates elongation of poly(A) tails by poly(A) polymerase I. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1501-5. PMID:10677490 doi:10.1073/pnas.040549897
↑ Sledjeski DD, Whitman C, Zhang A. Hfq is necessary for regulation by the untranslated RNA DsrA. J Bacteriol. 2001 Mar;183(6):1997-2005. PMID:11222598 doi:10.1128/JB.183.6.1997-2005.2001
↑ Guisbert E, Rhodius VA, Ahuja N, Witkin E, Gross CA. Hfq modulates the sigmaE-mediated envelope stress response and the sigma32-mediated cytoplasmic stress response in Escherichia coli. J Bacteriol. 2007 Mar;189(5):1963-73. Epub 2006 Dec 8. PMID:17158661 doi:10.1128/JB.01243-06
↑ Kim Y, Wood TK. Toxins Hha and CspD and small RNA regulator Hfq are involved in persister cell formation through MqsR in Escherichia coli. Biochem Biophys Res Commun. 2010 Jan 1;391(1):209-13. doi:, 10.1016/j.bbrc.2009.11.033. Epub 2009 Nov 10. PMID:19909729 doi:10.1016/j.bbrc.2009.11.033
↑ Beich-Frandsen M, Vecerek B, Sjoblom B, Blasi U, Djinovic-Carugo K. Structural analysis of full-length Hfq from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):536-40. Epub 2011 Apr 20. PMID:21543856 doi:10.1107/S174430911100786X

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3qhs"

@@ Line 1: / Line 1: @@
 ==Crystal structure of full-length Hfq from Escherichia coli==
-<StructureSection load='3qhs' size='340' side='right' caption='[[3qhs]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
+<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 [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QHS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3qhs]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qo3|3qo3]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qo3|3qo3]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4172, hfq, JW4130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b4172, hfq, JW4130 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhs OCA], [http://pdbe.org/3qhs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qhs RCSB], [http://www.ebi.ac.uk/pdbsum/3qhs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qhs ProSAT]</span></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 ==
-[[http://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>
+[[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 ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 3qhs" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Protein Hfq|Protein Hfq]]
 == References ==
 <references/>
@@ Line 24: / Line 27: @@
 </StructureSection>
 [[Category: Ecoli]]
+[[Category: Large Structures]]
 [[Category: Beich-Frandsen, M]]
 [[Category: Blaesi, U]]

3qhs

From Proteopedia

Revision as of 06:09, 8 June 2022

Crystal structure of full-length Hfq from Escherichia coli

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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