3mw6: Difference between revisions
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< | ==Crystal structure of NMB1681 from Neisseria meningitidis MC58, a FinO-like RNA chaperone== | ||
<StructureSection load='3mw6' size='340' side='right' caption='[[3mw6]], [[Resolution|resolution]] 2.21Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3mw6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimb Neimb]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2hxj 2hxj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MW6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MW6 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
-- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hxj|2hxj]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NMB1681 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=122586 NEIMB])</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=3mw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mw6 OCA], [http://pdbe.org/3mw6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mw6 RCSB], [http://www.ebi.ac.uk/pdbsum/3mw6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mw6 ProSAT]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mw/3mw6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3mw6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The conjugative transfer of F-like plasmids between bacteria is regulated by the plasmid-encoded RNA chaperone, FinO, which facilitates sense - antisense RNA interactions to regulate plasmid gene expression. FinO was thought to adopt a unique structure, however many putative homologs have been identified in microbial genomes and are considered members of the FinO_conjugation_repressor superfamily. We were interested in determining whether other members were also able to bind RNA and promote duplex formation, suggesting that this motif does indeed identify a putative RNA chaperone. We determined the crystal structure of the N. meningitidis MC58 protein NMB1681. It revealed striking similarity to FinO, with a conserved fold and a large, positively charged surface that could function in RNA interactions. Using assays developed to study FinO-FinP sRNA interactions, NMB1681, like FinO, bound tightly to FinP RNA stem-loops with short 5' and 3' single-stranded tails but not to ssRNA. It also was able to catalyze strand exchange between an RNA duplex and a complementary single-strand, and facilitated duplexing between complementary RNA hairpins. Finally, NMB1681 was able to rescue a finO deficiency and repress F plasmid conjugation. This study strongly suggests that NMB1681 is a FinO-like RNA chaperone that likely regulates gene expression through RNA-based mechanisms in N. meningitidis. | |||
N. meningitidis 1681 is a member of the FinO family of RNA chaperones.,Chaulk S, Lu J, Tan K, Arthur DC, Edwards RA, Frost LS, Joachimiak A, Glover JN RNA Biol. 2010 Nov 1;7(6):112-119. PMID:21045552<ref>PMID:21045552</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
<div class="pdbe-citations 3mw6" style="background-color:#fffaf0;"></div> | |||
[[Category: | == References == | ||
[[Category: Abdullah, J | <references/> | ||
[[Category: Duggan, E | __TOC__ | ||
[[Category: Joachimiak, A | </StructureSection> | ||
[[Category: | [[Category: Neimb]] | ||
[[Category: Tan, K | [[Category: Abdullah, J]] | ||
[[Category: Zhou, M | [[Category: Duggan, E]] | ||
[[Category: Joachimiak, A]] | |||
[[Category: Structural genomic]] | |||
[[Category: Tan, K]] | |||
[[Category: Zhou, M]] | |||
[[Category: Mcsg]] | [[Category: Mcsg]] | ||
[[Category: | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] | ||
Latest revision as of 16:30, 16 January 2019
Crystal structure of NMB1681 from Neisseria meningitidis MC58, a FinO-like RNA chaperoneCrystal structure of NMB1681 from Neisseria meningitidis MC58, a FinO-like RNA chaperone
Structural highlights
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 PubMedThe conjugative transfer of F-like plasmids between bacteria is regulated by the plasmid-encoded RNA chaperone, FinO, which facilitates sense - antisense RNA interactions to regulate plasmid gene expression. FinO was thought to adopt a unique structure, however many putative homologs have been identified in microbial genomes and are considered members of the FinO_conjugation_repressor superfamily. We were interested in determining whether other members were also able to bind RNA and promote duplex formation, suggesting that this motif does indeed identify a putative RNA chaperone. We determined the crystal structure of the N. meningitidis MC58 protein NMB1681. It revealed striking similarity to FinO, with a conserved fold and a large, positively charged surface that could function in RNA interactions. Using assays developed to study FinO-FinP sRNA interactions, NMB1681, like FinO, bound tightly to FinP RNA stem-loops with short 5' and 3' single-stranded tails but not to ssRNA. It also was able to catalyze strand exchange between an RNA duplex and a complementary single-strand, and facilitated duplexing between complementary RNA hairpins. Finally, NMB1681 was able to rescue a finO deficiency and repress F plasmid conjugation. This study strongly suggests that NMB1681 is a FinO-like RNA chaperone that likely regulates gene expression through RNA-based mechanisms in N. meningitidis. N. meningitidis 1681 is a member of the FinO family of RNA chaperones.,Chaulk S, Lu J, Tan K, Arthur DC, Edwards RA, Frost LS, Joachimiak A, Glover JN RNA Biol. 2010 Nov 1;7(6):112-119. PMID:21045552[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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