4c3d: Difference between revisions

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<StructureSection load='4c3d' size='340' side='right'caption='[[4c3d]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
<StructureSection load='4c3d' size='340' side='right'caption='[[4c3d]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4c3d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hrsva Hrsva]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3D FirstGlance]. <br>
<table><tr><td colspan='2'>[[4c3d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_respiratory_syncytial_virus_A2 Human respiratory syncytial virus A2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3D FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c3b|4c3b]], [[4c3e|4c3e]]</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=4c3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3d OCA], [https://pdbe.org/4c3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3d RCSB], [https://www.ebi.ac.uk/pdbsum/4c3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3d ProSAT]</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=4c3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3d OCA], [http://pdbe.org/4c3d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c3d RCSB], [http://www.ebi.ac.uk/pdbsum/4c3d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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> 
[[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;">
== Publication Abstract from PubMed ==
The M2-1 protein of the important pathogen human respiratory syncytial virus is a zinc-binding transcription antiterminator that is essential for viral gene expression. We present the crystal structure of full-length M2-1 protein in its native tetrameric form at a resolution of 2.5 A. The structure reveals that M2-1 forms a disk-like assembly with tetramerization driven by a long helix forming a four-helix bundle at its center, further stabilized by contact between the zinc-binding domain and adjacent protomers. The tetramerization helix is linked to a core domain responsible for RNA binding activity by a flexible region on which lie two functionally critical serine residues that are phosphorylated during infection. The crystal structure of a phosphomimetic M2-1 variant revealed altered charge density surrounding this flexible region although its position was unaffected. Structure-guided mutagenesis identified residues that contributed to RNA binding and antitermination activity, revealing a strong correlation between these two activities, and further defining the role of phosphorylation in M2-1 antitermination activity. The data we present here identify surfaces critical for M2-1 function that may be targeted by antiviral compounds.
 
Crystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylation.,Tanner SJ, Ariza A, Richard CA, Kyle HF, Dods RL, Blondot ML, Wu W, Trincao J, Trinh CH, Hiscox JA, Carroll MW, Silman NJ, Eleouet JF, Edwards TA, Barr JN Proc Natl Acad Sci U S A. 2014 Jan 16. PMID:24434552<ref>PMID:24434552</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4c3d" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hrsva]]
[[Category: Human respiratory syncytial virus A2]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ariza, A]]
[[Category: Ariza A]]
[[Category: Barr, J N]]
[[Category: Barr JN]]
[[Category: Carroll, M W]]
[[Category: Carroll MW]]
[[Category: Edwards, T A]]
[[Category: Edwards TA]]
[[Category: Eleouet, J F]]
[[Category: Eleouet JF]]
[[Category: Hiscox, J A]]
[[Category: Hiscox JA]]
[[Category: Richard, C A]]
[[Category: Richard CA]]
[[Category: Silman, N J]]
[[Category: Silman NJ]]
[[Category: Tanner, S J]]
[[Category: Tanner SJ]]
[[Category: Trincao, J]]
[[Category: Trincao J]]
[[Category: Wu, W]]
[[Category: Wu W]]
[[Category: M2-1 protein]]
[[Category: Viral protein]]

Revision as of 20:23, 7 September 2022

HRSV M2-1, P422 crystal formHRSV M2-1, P422 crystal form

Structural highlights

4c3d is a 2 chain structure with sequence from Human respiratory syncytial virus A2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

4c3d, resolution 2.52Å

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