3wbm
From Proteopedia
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==Crystal Structure of protein-RNA complex== | ==Crystal Structure of protein-RNA complex== | ||
| - | <StructureSection load='3wbm' size='340' side='right' caption='[[3wbm]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3wbm' size='340' side='right'caption='[[3wbm]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3wbm]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51178 Atcc 51178]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WBM FirstGlance]. <br> | <table><tr><td colspan='2'>[[3wbm]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_51178 Atcc 51178]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WBM FirstGlance]. <br> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ALBA1_SULSH ALBA1_SULSH]] Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. May be involved in DNA compaction. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.[HAMAP-Rule:MF_01122] | [[http://www.uniprot.org/uniprot/ALBA1_SULSH ALBA1_SULSH]] Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. May be involved in DNA compaction. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and functional stability of RNA, and, perhaps, ribosomes.[HAMAP-Rule:MF_01122] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Proteins of the Sac10b family are highly conserved in Archaea. Ssh10b, a member of the Sac10b family from the hyperthermophilic crenarchaeon Sulfolobus shibatae, binds to RNA in vivo. Here we show that binding by Ssh10b destabilizes RNA secondary structure. Structural analysis of Ssh10b in complex with a 25-bp RNA duplex containing local distortions reveals that Ssh10b binds the two RNA strands symmetrically as a tetramer with each dimer bound asymmetrically to a single RNA strand. Amino acid residues involved in double-stranded RNA binding are similar, but non-identical, to those in dsDNA binding. The dimer-dimer interaction mediated by the intermolecular beta-sheet appears to facilitate the destabilization of base pairing in the secondary structure of RNA. Our results suggest that proteins of the Sac10b family may play important roles in RNA transactions requiring destabilization of RNA secondary structure in Sulfolobus. | ||
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| + | Biochemical and structural insights into RNA binding by Ssh10b, a member of the highly conserved Sac10b protein family in Archaea.,Guo L, Ding J, Guo R, Hou Y, Wang DC, Huang L J Biol Chem. 2014 Jan 17;289(3):1478-90. doi: 10.1074/jbc.M113.521351. Epub 2013 , Dec 4. PMID:24307170<ref>PMID:24307170</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3wbm" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 51178]] | [[Category: Atcc 51178]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Ding, J]] | [[Category: Ding, J]] | ||
[[Category: Wang, D C]] | [[Category: Wang, D C]] | ||
Revision as of 09:55, 25 December 2019
Crystal Structure of protein-RNA complex
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