5fvc: Difference between revisions
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<StructureSection load='5fvc' size='340' side='right' caption='[[5fvc]], [[Resolution|resolution]] 4.17Å' scene=''> | <StructureSection load='5fvc' size='340' side='right' caption='[[5fvc]], [[Resolution|resolution]] 4.17Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fvc]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[5fvc]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Hmpv Hmpv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FVC FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fvd|5fvd]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fvd|5fvd]]</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=5fvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvc OCA], [http://pdbe.org/5fvc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fvc RCSB], [http://www.ebi.ac.uk/pdbsum/5fvc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvc 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=5fvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvc OCA], [http://pdbe.org/5fvc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fvc RCSB], [http://www.ebi.ac.uk/pdbsum/5fvc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvc ProSAT]</span></td></tr> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Hmpv]] | |||
[[Category: Bertinelli, M]] | [[Category: Bertinelli, M]] | ||
[[Category: Grimes, J M]] | [[Category: Grimes, J M]] | ||
Revision as of 23:31, 24 January 2018
Structure of RNA-bound decameric HMPV nucleoproteinStructure of RNA-bound decameric HMPV nucleoprotein
Structural highlights
Publication Abstract from PubMedNon-segmented, (-)RNA viruses cause serious human diseases. Human metapneumovirus (HMPV), an emerging pathogen of this order of viruses (Mononegavirales) is one of the main causes of respiratory tract illness in children. To help elucidate the assembly mechanism of the nucleocapsid (the viral RNA genome packaged by the nucleoprotein N) we present crystallographic structures of HMPV N in its assembled RNA-bound state and in a monomeric state, bound to the polymerase cofactor P. Our structures reveal molecular details of how P inhibits the self-assembly of N and how N transitions between the RNA-free and RNA-bound conformational state. Notably, we observe a role for the C-terminal extension of N in directly preventing premature uptake of RNA by inserting into the RNA-binding cleft.Our structures suggest a common mechanism of how the growth of the nucleocapsid is orchestrated, and highlight an interaction site representing an important target for antivirals. Nucleocapsid assembly in pneumoviruses is regulated by conformational switching of the N protein.,Renner M, Bertinelli M, Leyrat C, Paesen GC, Saraiva de Oliveira LF, Huiskonen JT, Grimes JM Elife. 2016 Feb 16;5. pii: e12627. doi: 10.7554/eLife.12627. PMID:26880565[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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