4xq3: Difference between revisions
New page: '''Unreleased structure''' The entry 4xq3 is ON HOLD until Paper Publication Authors: Bezerra, G.A., Martens, B., Kreuter, M.J., Grishkovskaya, I., Manica, M., Arkhipova, V., Blasi, U.,... |
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==Crystal structure of Sso-SmAP2== | |||
<StructureSection load='4xq3' size='340' side='right'caption='[[4xq3]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xq3]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_98/2 Saccharolobus solfataricus 98/2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XQ3 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]] 2.6Å</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=4xq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xq3 OCA], [https://pdbe.org/4xq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xq3 RCSB], [https://www.ebi.ac.uk/pdbsum/4xq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xq3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D0KRQ0_SACS9 D0KRQ0_SACS9] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sm and Sm-like proteins represent an evolutionarily conserved family with key roles in RNA metabolism. Sm-based regulation is diverse and can range in scope from eukaryotic mRNA splicing to bacterial quorum sensing, with at least one step in these processes being mediated by an RNA-associated molecular assembly built on Sm proteins. Despite the availability of several 3D-structures of Sm-like archaeal proteins (SmAPs), their function has remained elusive. The aim of this study was to shed light on the function of SmAP1 and SmAP2 of the crenarchaeon Sulfolobus solfataricus (Sso). Using co-purification followed by RNASeq different classes of non-coding RNAs and mRNAs were identified that co-purified either with both paralogues or solely with Sso-SmAP1 or Sso-SmAP2. The large number of associated intron-containing tRNAs and tRNA/rRNA modifying RNAs may suggest a role of the two Sso-SmAPs in tRNA/rRNA processing. Moreover, the 3D structure of Sso-SmAP2 was elucidated. Like Sso-SmAP1, Sso-SmAP2 forms homoheptamers. The binding of both proteins to distinct RNA substrates is discussed in terms of surface conservation, structural differences in the RNA binding sites and differences in the electrostatic surface potential of the two Sso-SmAP proteins. Taken together, this study may hint to common and different functions of both Sso-SmAPs in Sso RNA metabolism. | |||
The Heptameric SmAP1 and SmAP2 Proteins of the Crenarchaeon Sulfolobus Solfataricus Bind to Common and Distinct RNA Targets.,Martens B, Bezerra GA, Kreuter MJ, Grishkovskaya I, Manica A, Arkhipova V, Djinovic-Carugo K, Blasi U Life (Basel). 2015 Apr 21;5(2):1264-81. doi: 10.3390/life5021264. PMID:25905548<ref>PMID:25905548</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4xq3" style="background-color:#fffaf0;"></div> | ||
[[Category: Arkhipova | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Sm-like protein 3D structures|Sm-like protein 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Manica | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Saccharolobus solfataricus 98/2]] | |||
[[Category: Arkhipova V]] | |||
[[Category: Bezerra GA]] | |||
[[Category: Blasi U]] | |||
[[Category: Djinovic-Carugo K]] | |||
[[Category: Grishkovskaya I]] | |||
[[Category: Kreuter MJ]] | |||
[[Category: Manica M]] | |||
[[Category: Martens B]] | |||
Latest revision as of 13:50, 10 January 2024
Crystal structure of Sso-SmAP2Crystal structure of Sso-SmAP2
Structural highlights
FunctionPublication Abstract from PubMedSm and Sm-like proteins represent an evolutionarily conserved family with key roles in RNA metabolism. Sm-based regulation is diverse and can range in scope from eukaryotic mRNA splicing to bacterial quorum sensing, with at least one step in these processes being mediated by an RNA-associated molecular assembly built on Sm proteins. Despite the availability of several 3D-structures of Sm-like archaeal proteins (SmAPs), their function has remained elusive. The aim of this study was to shed light on the function of SmAP1 and SmAP2 of the crenarchaeon Sulfolobus solfataricus (Sso). Using co-purification followed by RNASeq different classes of non-coding RNAs and mRNAs were identified that co-purified either with both paralogues or solely with Sso-SmAP1 or Sso-SmAP2. The large number of associated intron-containing tRNAs and tRNA/rRNA modifying RNAs may suggest a role of the two Sso-SmAPs in tRNA/rRNA processing. Moreover, the 3D structure of Sso-SmAP2 was elucidated. Like Sso-SmAP1, Sso-SmAP2 forms homoheptamers. The binding of both proteins to distinct RNA substrates is discussed in terms of surface conservation, structural differences in the RNA binding sites and differences in the electrostatic surface potential of the two Sso-SmAP proteins. Taken together, this study may hint to common and different functions of both Sso-SmAPs in Sso RNA metabolism. The Heptameric SmAP1 and SmAP2 Proteins of the Crenarchaeon Sulfolobus Solfataricus Bind to Common and Distinct RNA Targets.,Martens B, Bezerra GA, Kreuter MJ, Grishkovskaya I, Manica A, Arkhipova V, Djinovic-Carugo K, Blasi U Life (Basel). 2015 Apr 21;5(2):1264-81. doi: 10.3390/life5021264. PMID:25905548[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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