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| | ==HRSV M2-1 core domain== | | ==HRSV M2-1 core domain== |
| - | <StructureSection load='5noh' size='340' side='right' caption='[[5noh]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='5noh' size='340' side='right'caption='[[5noh]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5noh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrsv Hrsv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NOH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NOH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5noh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_orthopneumovirus Human orthopneumovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NOH FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">M2, DZ88_50545gpM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11250 HRSV])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=5noh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5noh OCA], [http://pdbe.org/5noh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5noh RCSB], [http://www.ebi.ac.uk/pdbsum/5noh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5noh 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=5noh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5noh OCA], [https://pdbe.org/5noh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5noh RCSB], [https://www.ebi.ac.uk/pdbsum/5noh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5noh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/M21_HRSVA M21_HRSVA] Acts as a transcriptional elongation factor to prevent premature termination during transcription thus allowing complete synthesis of RSV mRNAs. Functions also as a processivity and antitermination factor to permit transit of the polymerase through intergenic regions to access promoter distal genes. Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding. Also, can activate NF-kappa-B through association with host RELA.<ref>PMID:8552680</ref> <ref>PMID:9420254</ref> <ref>PMID:10364337</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5noh" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5noh" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Elongation factor 3D structures|Elongation factor 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hrsv]] | + | [[Category: Human orthopneumovirus]] |
| - | [[Category: Hernandez, Y Almeida]] | + | [[Category: Large Structures]] |
| - | [[Category: Josts, I]] | + | [[Category: Almeida Hernandez Y]] |
| - | [[Category: Molina, I G]] | + | [[Category: Josts I]] |
| - | [[Category: Prat-Gay, G de]] | + | [[Category: Molina IG]] |
| - | [[Category: Tidow, H]] | + | [[Category: Tidow H]] |
| - | [[Category: Protein]] | + | [[Category: De Prat-Gay G]] |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
M21_HRSVA Acts as a transcriptional elongation factor to prevent premature termination during transcription thus allowing complete synthesis of RSV mRNAs. Functions also as a processivity and antitermination factor to permit transit of the polymerase through intergenic regions to access promoter distal genes. Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding. Also, can activate NF-kappa-B through association with host RELA.[1] [2] [3]
Publication Abstract from PubMed
Human syncytial respiratory virus is a nonsegmented negative-strand RNA virus with serious implications for respiratory disease in infants, and has recently been reclassified into a new family, Pneumoviridae. One of the main reasons for this classification is the unique presence of a transcriptional antiterminator, called M2-1. The puzzling mechanism of action of M2-1, which is a rarity among antiterminators in viruses and is part of the RNA polymerase complex, relies on dissecting the structure and function of this multidomain tetramer. The RNA-binding activity is located in a monomeric globular `core' domain, a high-resolution crystal structure of which is now presented. The structure reveals a compact domain which is superimposable on the full-length M2-1 tetramer, with additional electron density for the C-terminal tail that was not observed in the previous models. Moreover, its folding stability was determined through chemical denaturation, which shows that the secondary and tertiary structure unfold concomitantly, which is indicative of a two-state equilibrium. These results constitute a further step in the understanding of this unique RNA-binding domain, for which there is no sequence or structural counterpart outside this virus family, in addition to its implications in transcription regulation and its likeliness as an antiviral target.
Structure and stability of the Human respiratory syncytial virus M2-1 RNA-binding core domain reveals a compact and cooperative folding unit.,Molina IG, Josts I, Almeida Hernandez Y, Esperante S, Salgueiro M, Garcia Alai MM, de Prat-Gay G, Tidow H Acta Crystallogr F Struct Biol Commun. 2018 Jan 1;74(Pt 1):23-30. doi:, 10.1107/S2053230X17017381. Epub 2017 Dec 15. PMID:29372904[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Collins PL, Hill MG, Cristina J, Grosfeld H. Transcription elongation factor of respiratory syncytial virus, a nonsegmented negative-strand RNA virus. Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):81-5. PMID:8552680
- ↑ Hardy RW, Wertz GW. The product of the respiratory syncytial virus M2 gene ORF1 enhances readthrough of intergenic junctions during viral transcription. J Virol. 1998 Jan;72(1):520-6. PMID:9420254
- ↑ Fearns R, Collins PL. Role of the M2-1 transcription antitermination protein of respiratory syncytial virus in sequential transcription. J Virol. 1999 Jul;73(7):5852-64. PMID:10364337
- ↑ Molina IG, Josts I, Almeida Hernandez Y, Esperante S, Salgueiro M, Garcia Alai MM, de Prat-Gay G, Tidow H. Structure and stability of the Human respiratory syncytial virus M2-1 RNA-binding core domain reveals a compact and cooperative folding unit. Acta Crystallogr F Struct Biol Commun. 2018 Jan 1;74(Pt 1):23-30. doi:, 10.1107/S2053230X17017381. Epub 2017 Dec 15. PMID:29372904 doi:http://dx.doi.org/10.1107/S2053230X17017381
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