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2yjv

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Revision as of 07:59, 4 August 2016

Crystal structure of E. coli regulator of ribonuclease activity A (RraA) bound to fragment of DEAD-box protein RhlB

Structural highlights

2yjv is a 14 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1q5x, 2yjt
Activity:	DNA helicase, with EC number 3.6.4.12
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RRAA_ECOLI] Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Members of the DEAD-box family of RNA helicases contribute to virtually every aspect of RNA metabolism, in organisms from all domains of life. Many of these helicases are constituents of multi-component assemblies, and their interactions with partner proteins within the complexes underpin their activities and biological function. In Escherichia coli the DEAD-box helicase RhlB is a component of the multi-enzyme RNA degradosome assembly, and its interaction with the core ribonuclease RNase E boosts the ATP-dependent activity of the helicase (1,2). Earlier studies have identified the regulator of ribonuclease activity A (RraA) as a potential interaction partner of both RNase E and RhlB (3). We present structural and biochemical evidence showing how RraA can bind to, and modulate the activity of RhlB and another E. coli DEAD-box enzyme, SrmB. Crystallographic structures are presented of RraA in complex with a portion of the natively unstructured C-terminal tail of RhlB at 2.8 A resolution, and in complex with the C-terminal RecA-like domain of SrmB at 2.9 A. The models suggest two distinct mechanisms by which RraA might modulate the activity of these and potentially other helicases.

Potential regulatory interactions of Escherichia coli RraA protein with DEAD-box helicases.,Pietras Z, Hardwick SW, Swiezewski S, Luisi BF J Biol Chem. 2013 Sep 17. PMID:24045937^[6]

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

References

↑ Lee K, Zhan X, Gao J, Qiu J, Feng Y, Meganathan R, Cohen SN, Georgiou G. RraA. a protein inhibitor of RNase E activity that globally modulates RNA abundance in E. coli. Cell. 2003 Sep 5;114(5):623-34. PMID:13678585
↑ Yeom JH, Lee K. RraA rescues Escherichia coli cells over-producing RNase E from growth arrest by modulating the ribonucleolytic activity. Biochem Biophys Res Commun. 2006 Jul 14;345(4):1372-6. Epub 2006 May 11. PMID:16725107 doi:10.1016/j.bbrc.2006.05.018
↑ Gao J, Lee K, Zhao M, Qiu J, Zhan X, Saxena A, Moore CJ, Cohen SN, Georgiou G. Differential modulation of E. coli mRNA abundance by inhibitory proteins that alter the composition of the degradosome. Mol Microbiol. 2006 Jul;61(2):394-406. Epub 2006 Jun 12. PMID:16771842 doi:10.1111/j.1365-2958.2006.05246.x
↑ Yeom JH, Go H, Shin E, Kim HL, Han SH, Moore CJ, Bae J, Lee K. Inhibitory effects of RraA and RraB on RNAse E-related enzymes imply conserved functions in the regulated enzymatic cleavage of RNA. FEMS Microbiol Lett. 2008 Aug;285(1):10-5. doi: 10.1111/j.1574-6968.2008.01205.x., Epub 2008 May 28. PMID:18510556 doi:10.1111/j.1574-6968.2008.01205.x
↑ Gorna MW, Pietras Z, Tsai YC, Callaghan AJ, Hernandez H, Robinson CV, Luisi BF. The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome. RNA. 2010 Jan 27. PMID:20106955 doi:rna.1858010
↑ Pietras Z, Hardwick SW, Swiezewski S, Luisi BF. Potential regulatory interactions of Escherichia coli RraA protein with DEAD-box helicases. J Biol Chem. 2013 Sep 17. PMID:24045937 doi:10.1074/jbc.M113.502146

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2yjv"

@@ Line 1: / Line 1: @@
 ==Crystal structure of E. coli regulator of ribonuclease activity A (RraA) bound to fragment of DEAD-box protein RhlB==
 <StructureSection load='2yjv' size='340' side='right' caption='[[2yjv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q5x|1q5x]], [[2yjt|2yjt]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></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=2yjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yjv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yjv RCSB], [http://www.ebi.ac.uk/pdbsum/2yjv PDBsum]</span></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=2yjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yjv OCA], [http://pdbe.org/2yjv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yjv RCSB], [http://www.ebi.ac.uk/pdbsum/2yjv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yjv ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2yjv" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2yjv

From Proteopedia

Revision as of 07:59, 4 August 2016

Crystal structure of E. coli regulator of ribonuclease activity A (RraA) bound to fragment of DEAD-box protein RhlB

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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