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| | <StructureSection load='2yjt' size='340' side='right'caption='[[2yjt]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='2yjt' size='340' side='right'caption='[[2yjt]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2yjt]] is a 4 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=2YJT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YJT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2yjt]] is a 4 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=2YJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YJT FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yjv|2yjv]]</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;'>[[2yjv|2yjv]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </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=2yjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yjt OCA], [http://pdbe.org/2yjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yjt RCSB], [http://www.ebi.ac.uk/pdbsum/2yjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yjt 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=2yjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yjt OCA], [https://pdbe.org/2yjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yjt RCSB], [https://www.ebi.ac.uk/pdbsum/2yjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yjt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/D8AM26_ECOLX D8AM26_ECOLX]] 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 (By similarity).[HAMAP-Rule:MF_00471][SAAS:SAAS005493_004_044335] [[http://www.uniprot.org/uniprot/SRMB_ECOLI SRMB_ECOLI]] DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity. Acts before DeaD.<ref>PMID:12787353</ref> <ref>PMID:15196029</ref> <ref>PMID:15148362</ref> | + | [[https://www.uniprot.org/uniprot/D8AM26_ECOLX D8AM26_ECOLX]] 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 (By similarity).[HAMAP-Rule:MF_00471][SAAS:SAAS005493_004_044335] [[https://www.uniprot.org/uniprot/SRMB_ECOLI SRMB_ECOLI]] DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity. Acts before DeaD.<ref>PMID:12787353</ref> <ref>PMID:15196029</ref> <ref>PMID:15148362</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Helicase|Helicase]] | + | *[[Helicase 3D structures|Helicase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[D8AM26_ECOLX] 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 (By similarity).[HAMAP-Rule:MF_00471][SAAS:SAAS005493_004_044335] [SRMB_ECOLI] DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity. Acts before DeaD.[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Charollais J, Pflieger D, Vinh J, Dreyfus M, Iost I. The DEAD-box RNA helicase SrmB is involved in the assembly of 50S ribosomal subunits in Escherichia coli. Mol Microbiol. 2003 Jun;48(5):1253-65. PMID:12787353
- ↑ Bizebard T, Ferlenghi I, Iost I, Dreyfus M. Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases. Biochemistry. 2004 Jun 22;43(24):7857-66. PMID:15196029 doi:10.1021/bi049852s
- ↑ Charollais J, Dreyfus M, Iost I. CsdA, a cold-shock RNA helicase from Escherichia coli, is involved in the biogenesis of 50S ribosomal subunit. Nucleic Acids Res. 2004 May 17;32(9):2751-9. Print 2004. PMID:15148362 doi:10.1093/nar/gkh603
- ↑ 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
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