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| | <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 [https://en.wikipedia.org/wiki/Saccharolobus_shibatae Saccharolobus shibatae] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3WBM FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">albA1, ssh10b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2286 ATCC 51178])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=3wbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wbm OCA], [http://pdbe.org/3wbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wbm RCSB], [http://www.ebi.ac.uk/pdbsum/3wbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wbm ProSAT]</span></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=3wbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wbm OCA], [https://pdbe.org/3wbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wbm RCSB], [https://www.ebi.ac.uk/pdbsum/3wbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wbm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == 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] | + | [https://www.uniprot.org/uniprot/ALBA1_SACSH ALBA1_SACSH] 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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 51178]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ding, J]] | + | [[Category: Saccharolobus shibatae]] |
| - | [[Category: Wang, D C]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Dna/rna binding]] | + | [[Category: Ding J]] |
| - | [[Category: Protein-rna complex]] | + | [[Category: Wang DC]] |
| - | [[Category: Rna binding protein-rna complex]]
| + | |
| Structural highlights
Function
ALBA1_SACSH 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.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guo L, Ding J, Guo R, Hou Y, Wang DC, Huang L. Biochemical and structural insights into RNA binding by Ssh10b, a member of the highly conserved Sac10b protein family in Archaea. J Biol Chem. 2014 Jan 17;289(3):1478-90. doi: 10.1074/jbc.M113.521351. Epub 2013 , Dec 4. PMID:24307170 doi:http://dx.doi.org/10.1074/jbc.M113.521351
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