4hl8: Difference between revisions
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<StructureSection load='4hl8' size='340' side='right'caption='[[4hl8]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='4hl8' size='340' side='right'caption='[[4hl8]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hl8]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4hl8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HL8 FirstGlance]. <br> | ||
</td></tr> | </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=4hl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hl8 OCA], [https://pdbe.org/4hl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hl8 RCSB], [https://www.ebi.ac.uk/pdbsum/4hl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hl8 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MVP_RAT MVP_RAT] Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
The vault particle, with a molecular weight of about 10 MDa, is the largest ribonucleoprotein that has been described. The X-ray structure of intact rat vault has been solved at a resolution of 3.5 A [Tanaka et al. (2009), Science, 323, 384-388], showing an overall barrel-shaped architecture organized into two identical moieties, each consisting of 39 copies of the major vault protein (MVP). The model deposited in the PDB includes 39 MVP copies (half a vault) in the crystal asymmetric unit. A 2.1 A resolution structure of the seven N-terminal repeats (R1-7) of MVP has also been determined [Querol-Audi et al. (2009), EMBO J. 28, 3450-3457], revealing important discrepancies with respect to the MVP models for repeats R1 and R2. Here, the re-refinement of the vault structure by incorporating the high-resolution information available for the R1-7 domains, using the deformable elastic network (DEN) approach and maintaining strict 39-fold noncrystallographic symmetry is reported. The new refinement indicates that at the resolution presently available the MVP shell can be described well as only one independent subunit organized with perfect D39 molecular symmetry. This refinement reveals that significant rearrangements occur in the N-terminus of MVP during the closing of the two vault halves and that the 39-fold symmetry breaks in the cap region. These results reflect the highly dynamic nature of the vault structure and represent a necessary step towards a better understanding of the biology and regulation of this particle. | |||
New features of vault architecture and dynamics revealed by novel refinement using the deformable elastic network approach.,Casanas A, Querol-Audi J, Guerra P, Pous J, Tanaka H, Tsukihara T, Verdaguer N, Fita I Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):1054-61. doi:, 10.1107/S0907444913004472. Epub 2013 May 14. PMID:23695250<ref>PMID:23695250</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4hl8" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4hl8" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Casanas | [[Category: Casanas A]] | ||
[[Category: Fita | [[Category: Fita I]] | ||
[[Category: Guerra | [[Category: Guerra P]] | ||
[[Category: Pous | [[Category: Pous J]] | ||
[[Category: Querol-Audi | [[Category: Querol-Audi J]] | ||
[[Category: Tanaka | [[Category: Tanaka H]] | ||
[[Category: Tsukihara | [[Category: Tsukihara T]] | ||
[[Category: Verdaguer | [[Category: Verdaguer V]] | ||
Revision as of 11:24, 3 November 2022
Re-refinement of the vault ribonucleoprotein particleRe-refinement of the vault ribonucleoprotein particle
Structural highlights
FunctionMVP_RAT Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates INFG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases (By similarity). Publication Abstract from PubMedThe vault particle, with a molecular weight of about 10 MDa, is the largest ribonucleoprotein that has been described. The X-ray structure of intact rat vault has been solved at a resolution of 3.5 A [Tanaka et al. (2009), Science, 323, 384-388], showing an overall barrel-shaped architecture organized into two identical moieties, each consisting of 39 copies of the major vault protein (MVP). The model deposited in the PDB includes 39 MVP copies (half a vault) in the crystal asymmetric unit. A 2.1 A resolution structure of the seven N-terminal repeats (R1-7) of MVP has also been determined [Querol-Audi et al. (2009), EMBO J. 28, 3450-3457], revealing important discrepancies with respect to the MVP models for repeats R1 and R2. Here, the re-refinement of the vault structure by incorporating the high-resolution information available for the R1-7 domains, using the deformable elastic network (DEN) approach and maintaining strict 39-fold noncrystallographic symmetry is reported. The new refinement indicates that at the resolution presently available the MVP shell can be described well as only one independent subunit organized with perfect D39 molecular symmetry. This refinement reveals that significant rearrangements occur in the N-terminus of MVP during the closing of the two vault halves and that the 39-fold symmetry breaks in the cap region. These results reflect the highly dynamic nature of the vault structure and represent a necessary step towards a better understanding of the biology and regulation of this particle. New features of vault architecture and dynamics revealed by novel refinement using the deformable elastic network approach.,Casanas A, Querol-Audi J, Guerra P, Pous J, Tanaka H, Tsukihara T, Verdaguer N, Fita I Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):1054-61. doi:, 10.1107/S0907444913004472. Epub 2013 May 14. PMID:23695250[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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