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7k9c

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Current revision (14:55, 6 March 2024) (edit) (undo)
 
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<StructureSection load='7k9c' size='340' side='right'caption='[[7k9c]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
<StructureSection load='7k9c' size='340' side='right'caption='[[7k9c]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7k9c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K9C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7k9c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K9C FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7k9b|7k9b]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></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=7k9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k9c OCA], [https://pdbe.org/7k9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k9c RCSB], [https://www.ebi.ac.uk/pdbsum/7k9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k9c 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=7k9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k9c OCA], [https://pdbe.org/7k9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k9c RCSB], [https://www.ebi.ac.uk/pdbsum/7k9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k9c ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9KGD7_HALH5 Q9KGD7_HALH5]
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The OLE (ornate, large, and extremophilic) RNA class is one of the most complex and well-conserved bacterial noncoding RNAs known to exist. This RNA is known to be important for bacterial responses to stress caused by short-chain alcohols, cold, and elevated Mg(2+) concentrations. These biological functions have been shown to require the formation of a ribonucleoprotein (RNP) complex including at least two protein partners: OLE-associated protein A (OapA) and OLE-associated protein B (OapB). OapB directly binds OLE RNA with high-affinity and specificity and is believed to assist in assembling the functional OLE RNP complex. To provide the atomic details of OapB-OLE RNA interaction and to potentially reveal previously uncharacterized protein-RNA interfaces, we determined the structure of OapB from Bacillus halodurans alone and in complex with an OLE RNA fragment at resolutions of 1.0 A and 2.0 A, respectively. The structure of OapB exhibits a K-shaped overall architecture wherein its conserved KOW motif and additional unique structural elements of OapB form a bipartite RNA-binding surface that docks to the P13 hairpin and P12.2 helix of OLE RNA. These high-resolution structures elucidate the molecular contacts used by OapB to form a stable RNP complex and explain the high conservation of sequences and structural features at the OapB-OLE RNA-binding interface. These findings provide insight into the role of OapB in the assembly and biological function of OLE RNP complex and can guide the exploration of additional possible OLE RNA-binding interactions present in OapB.
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Structure of a bacterial OapB protein with its OLE RNA target gives insights into the architecture of the OLE ribonucleoprotein complex.,Yang Y, Harris KA, Widner DL, Breaker RR Proc Natl Acad Sci U S A. 2021 Mar 2;118(9). pii: 2020393118. doi:, 10.1073/pnas.2020393118. PMID:33619097<ref>PMID:33619097</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7k9c" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alkalihalobacillus halodurans C-125]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Breaker, R R]]
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[[Category: Breaker RR]]
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[[Category: Yang, Y]]
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[[Category: Yang Y]]
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[[Category: Ole rna]]
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[[Category: Ribonucleoprotein complex]]
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[[Category: Rna]]
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[[Category: Rna binding protein]]
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Current revision

Crystal structure of Bacillus halodurans OapB (iodine-derivative) at 1.0 A

PDB ID 7k9c

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