5dsd: Difference between revisions
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<StructureSection load='5dsd' size='340' side='right'caption='[[5dsd]], [[Resolution|resolution]] 2.31Å' scene=''> | <StructureSection load='5dsd' size='340' side='right'caption='[[5dsd]], [[Resolution|resolution]] 2.31Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5dsd]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5dsd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bundibugyo_ebolavirus Bundibugyo ebolavirus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5cij 5cij]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DSD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.31Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=5dsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dsd OCA], [https://pdbe.org/5dsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dsd RCSB], [https://www.ebi.ac.uk/pdbsum/5dsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dsd ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B8XCM7_9MONO B8XCM7_9MONO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bundibugyo ebolavirus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Baker | [[Category: Baker L]] | ||
[[Category: Derewenda | [[Category: Derewenda U]] | ||
[[Category: Derewenda | [[Category: Derewenda ZS]] | ||
[[Category: Handing | [[Category: Handing KB]] | ||
[[Category: Utepbergenov | [[Category: Utepbergenov D]] | ||
Latest revision as of 00:57, 29 June 2023
The crystal structure of the C-terminal domain of Ebola (Bundibugyo) nucleoproteinThe crystal structure of the C-terminal domain of Ebola (Bundibugyo) 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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