3lyf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:22, 21 February 2024) (edit) (undo)
 
Line 1: Line 1:
==Crystal Structure of the Rift Valley Fever Virus Nucleocapsid Protein==
==Crystal Structure of the Rift Valley Fever Virus Nucleocapsid Protein==
-
<StructureSection load='3lyf' size='340' side='right' caption='[[3lyf]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
+
<StructureSection load='3lyf' size='340' side='right'caption='[[3lyf]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3lyf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Rvfv Rvfv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LYF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LYF FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3lyf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rift_Valley_fever_virus Rift Valley fever virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LYF FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 1.93&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11588 RVFV])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3lyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lyf OCA], [http://pdbe.org/3lyf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lyf RCSB], [http://www.ebi.ac.uk/pdbsum/3lyf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lyf 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=3lyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lyf OCA], [https://pdbe.org/3lyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lyf RCSB], [https://www.ebi.ac.uk/pdbsum/3lyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lyf ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/NCAP_RVFV NCAP_RVFV] Encapsidates the genomic RNA, protecting it from nucleases (Probable) (PubMed:20547879). Displays high affinity for single-stranded nucleic acid (PubMed:23129612). The encapsidated genomic RNA is termed the nucleocapsid (NC) or ribonucleoprotein (PubMed:20547879). The ribonucleoprotein has a non-helical structure (PubMed:20547879). Serves as template for viral transcription and replication (By similarity). After replication, the nucleocapsid is recruited to the host Golgi apparatus by glycoprotein Gn for packaging into virus particles (By similarity).[UniProtKB:P21700]<ref>PMID:20547879</ref> <ref>PMID:23129612</ref> <ref>PMID:34960686</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 18: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lyf ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lyf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
Rift Valley fever virus (RVFV) is a negative-sense RNA virus (genus Phlebovirus, family Bunyaviridae) that infects livestock and humans and is endemic to sub-Saharan Africa. Like all negative-sense viruses, the segmented RNA genome of RVFV is encapsidated by a nucleocapsid protein (N). The 1.93-A crystal structure of RVFV N and electron micrographs of ribonucleoprotein (RNP) reveal an encapsidated genome of substantially different organization than in other negative-sense RNA virus families. The RNP polymer, viewed in electron micrographs of both virus RNP and RNP reconstituted from purified N with a defined RNA, has an extended structure without helical symmetry. N-RNA species of approximately 100-kDa apparent molecular weight and heterogeneous composition were obtained by exhaustive ribonuclease treatment of virus RNP, by recombinant expression of N, and by reconstitution from purified N and an RNA oligomer. RNA-free N, obtained by denaturation and refolding, has a novel all-helical fold that is compact and well ordered at both the N and C termini. Unlike N of other negative-sense RNA viruses, RVFV N has no positively charged surface cleft for RNA binding and no protruding termini or loops to stabilize a defined N-RNA oligomer or RNP helix. A potential protein interaction site was identified in a conserved hydrophobic pocket. The nonhelical appearance of phlebovirus RNP, the heterogeneous approximately 100-kDa N-RNA multimer, and the N fold differ substantially from the RNP and N of other negative-sense RNA virus families and provide valuable insights into the structure of the encapsidated phlebovirus genome.
 
- 
-
Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation.,Raymond DD, Piper ME, Gerrard SR, Smith JL Proc Natl Acad Sci U S A. 2010 Jun 14. PMID:20547879<ref>PMID:20547879</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 3lyf" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Rvfv]]
+
[[Category: Large Structures]]
-
[[Category: Raymond, D D]]
+
[[Category: Rift Valley fever virus]]
-
[[Category: Smith, J L]]
+
[[Category: Raymond DD]]
-
[[Category: N protein]]
+
[[Category: Smith JL]]
-
[[Category: Nucleocapsid protein]]
+
-
[[Category: Ribonucleoprotein]]
+
-
[[Category: Rift valley fever virus]]
+
-
[[Category: Viral nucleoprotein]]
+
-
[[Category: Viral protein]]
+

Current revision

Crystal Structure of the Rift Valley Fever Virus Nucleocapsid Protein

PDB ID 3lyf

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools