3l7z

From Proteopedia

(Difference between revisions)

Revision as of 21:10, 25 December 2014

Crystal structure of the S. solfataricus archaeal exosome

Structural highlights

3l7z is a 9 chain structure with sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	C20_023, Rrp41/42/4, SSO0732 (Sulfolobus solfataricus), SSO0735 (Sulfolobus solfataricus), C20_026, SSO0736 (Sulfolobus solfataricus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[ECX2_SULSO] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential). [ECR1_SULSO] Probably involved in degradation of a variety of RNA species; could act a RNA-binding component of the exosome (Potential). [ECX1_SULSO] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: The exosome complex is an essential RNA 3'-end processing and degradation machinery. In archaeal organisms, the exosome consists of a catalytic ring and an RNA-binding ring, both of which were previously reported to assume three-fold symmetry. METHODOLOGY/PRINCIPAL FINDINGS: Here we report an asymmetric 2.9 A Sulfolobus solfataricus archaeal exosome structure in which the three-fold symmetry is broken due to combined rigid body and thermal motions mainly within the RNA-binding ring. Since increased conformational flexibility was also observed in the RNA-binding ring of the related bacterial PNPase, we speculate that this may reflect an evolutionarily conserved mechanism to accommodate diverse RNA substrates for degradation. CONCLUSION/SIGNIFICANCE: This study clearly shows the dynamic structures within the RNA-binding domains, which provides additional insights on mechanism of asymmetric RNA binding and processing.

Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring.,Lu C, Ding F, Ke A PLoS One. 2010 Jan 15;5(1):e8739. PMID:20090900^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lu C, Ding F, Ke A. Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring. PLoS One. 2010 Jan 15;5(1):e8739. PMID:20090900 doi:10.1371/journal.pone.0008739

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3l7z"

@@ Line 7: / Line 7: @@
 <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=3l7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l7z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l7z RCSB], [http://www.ebi.ac.uk/pdbsum/3l7z PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ECX2_SULSO ECX2_SULSO]] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential). [[http://www.uniprot.org/uniprot/ECR1_SULSO ECR1_SULSO]] Probably involved in degradation of a variety of RNA species; could act a RNA-binding component of the exosome (Potential). [[http://www.uniprot.org/uniprot/ECX1_SULSO ECX1_SULSO]] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3l7z

From Proteopedia

Revision as of 21:10, 25 December 2014

Crystal structure of the S. solfataricus archaeal exosome

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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