5e2x: Difference between revisions
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The entry 5e2x is | ==The crystal structure of the C-terminal domain of Ebola (Tai Forest) nucleoprotein== | ||
<StructureSection load='5e2x' size='340' side='right'caption='[[5e2x]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5e2x]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Tai_Forest_ebolavirus Tai Forest ebolavirus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5cii 5cii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E2X FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene></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=5e2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e2x OCA], [https://pdbe.org/5e2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e2x RCSB], [https://www.ebi.ac.uk/pdbsum/5e2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e2x ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B8XCN6_9MONO B8XCN6_9MONO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Filoviridae family of negative-sense, single-stranded RNA (ssRNA) viruses is comprised of two species of Marburgvirus (MARV and RAVV) and five species of Ebolavirus, i.e. Zaire (EBOV), Reston (RESTV), Sudan (SUDV), Tai Forest (TAFV) and Bundibugyo (BDBV). In each of these viruses the ssRNA encodes seven distinct proteins. One of them, the nucleoprotein (NP), is the most abundant viral protein in the infected cell and within the viral nucleocapsid. It is tightly associated with the viral RNA in the nucleocapsid, and during the lifecycle of the virus is essential for transcription, RNA replication, genome packaging and nucleocapsid assembly prior to membrane encapsulation. The structure of the unique C-terminal globular domain of the NP from EBOV has recently been determined and shown to be structurally unrelated to any other known protein [Dziubanska et al. (2014), Acta Cryst. D70, 2420-2429]. In this paper, a study of the C-terminal domains from the NP from the remaining four species of Ebolavirus, as well as from the MARV strain of Marburgvirus, is reported. As expected, the crystal structures of the BDBV and TAFV proteins show high structural similarity to that from EBOV, while the MARV protein behaves like a molten globule with a core residual structure that is significantly different from that of the EBOV protein. | |||
Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses.,Baker LE, Ellena JF, Handing KB, Derewenda U, Utepbergenov D, Engel DA, Derewenda ZS Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):49-58. doi:, 10.1107/S2059798315021439. Epub 2016 Jan 1. PMID:26894534<ref>PMID:26894534</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Baker | <div class="pdbe-citations 5e2x" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Derewenda | ==See Also== | ||
[[Category: | *[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]] | ||
[[Category: Utepbergenov | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Tai Forest ebolavirus]] | |||
[[Category: Baker LE]] | |||
[[Category: Derewenda U]] | |||
[[Category: Derewenda ZS]] | |||
[[Category: Handing KB]] | |||
[[Category: Utepbergenov D]] | |||
Latest revision as of 09:11, 5 July 2023
The crystal structure of the C-terminal domain of Ebola (Tai Forest) nucleoproteinThe crystal structure of the C-terminal domain of Ebola (Tai Forest) nucleoprotein
Structural highlights
FunctionPublication Abstract from PubMedThe Filoviridae family of negative-sense, single-stranded RNA (ssRNA) viruses is comprised of two species of Marburgvirus (MARV and RAVV) and five species of Ebolavirus, i.e. Zaire (EBOV), Reston (RESTV), Sudan (SUDV), Tai Forest (TAFV) and Bundibugyo (BDBV). In each of these viruses the ssRNA encodes seven distinct proteins. One of them, the nucleoprotein (NP), is the most abundant viral protein in the infected cell and within the viral nucleocapsid. It is tightly associated with the viral RNA in the nucleocapsid, and during the lifecycle of the virus is essential for transcription, RNA replication, genome packaging and nucleocapsid assembly prior to membrane encapsulation. The structure of the unique C-terminal globular domain of the NP from EBOV has recently been determined and shown to be structurally unrelated to any other known protein [Dziubanska et al. (2014), Acta Cryst. D70, 2420-2429]. In this paper, a study of the C-terminal domains from the NP from the remaining four species of Ebolavirus, as well as from the MARV strain of Marburgvirus, is reported. As expected, the crystal structures of the BDBV and TAFV proteins show high structural similarity to that from EBOV, while the MARV protein behaves like a molten globule with a core residual structure that is significantly different from that of the EBOV protein. Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses.,Baker LE, Ellena JF, Handing KB, Derewenda U, Utepbergenov D, Engel DA, Derewenda ZS Acta Crystallogr D Struct Biol. 2016 Jan;72(Pt 1):49-58. doi:, 10.1107/S2059798315021439. Epub 2016 Jan 1. PMID:26894534[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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