3ahu: Difference between revisions

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<StructureSection load='3ahu' size='340' side='right'caption='[[3ahu]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3ahu' size='340' side='right'caption='[[3ahu]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ahu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AHU FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ahu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AHU FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU17340, hfq, ymaH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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]] 2.2&#8491;</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=3ahu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ahu OCA], [https://pdbe.org/3ahu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ahu RCSB], [https://www.ebi.ac.uk/pdbsum/3ahu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ahu 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=3ahu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ahu OCA], [https://pdbe.org/3ahu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ahu RCSB], [https://www.ebi.ac.uk/pdbsum/3ahu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ahu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HFQ_BACSU HFQ_BACSU]] RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.[HAMAP-Rule:MF_00436]  
[https://www.uniprot.org/uniprot/HFQ_BACSU HFQ_BACSU] RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.[HAMAP-Rule:MF_00436]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Hfq protein is a hexameric RNA-binding protein which regulates gene expression by binding to RNA under the influence of diverse environmental stresses. Its ring structure binds various types of RNA, including mRNA and sRNA. RNA-bound structures of Hfq from Escherichia coli and Staphylococcus aureus have been revealed to have poly(A) RNA at the distal site and U-rich RNA at the proximal site, respectively. Here, crystals of a complex of the Bacillus subtilis Hfq protein with an A/G-repeat 7-mer RNA (Hfq-RNA) that were prepared using the hanging-drop vapour-diffusion technique are reported. The type 1 Hfq-RNA crystals belonged to space group I422, with unit-cell parameters a = b = 123.70, c = 119.13 A, while the type 2 Hfq-RNA crystals belonged to space group F222, with unit-cell parameters a = 91.92, b = 92.50, c = 114.92 A. Diffraction data were collected to a resolution of 2.20 A from both crystal forms. The hexameric structure of the Hfq protein was clearly shown by self-rotation analysis.
 
Expression, crystallization and preliminary crystallographic analysis of RNA-binding protein Hfq (YmaH) from Bacillus subtilis in complex with an RNA aptamer.,Baba S, Someya T, Kawai G, Nakamura K, Kumasaka T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 May 1;66(Pt, 5):563-6. Epub 2010 Apr 30. PMID:20445260<ref>PMID:20445260</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ahu" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Protein Hfq|Protein Hfq]]
*[[Protein Hfq 3D structures|Protein Hfq 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Vibrio subtilis ehrenberg 1835]]
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Baba, S]]
[[Category: Baba S]]
[[Category: Kawai, G]]
[[Category: Kawai G]]
[[Category: Kumasaka, T]]
[[Category: Kumasaka T]]
[[Category: Nakamura, K]]
[[Category: Nakamura K]]
[[Category: Someya, T]]
[[Category: Someya T]]
[[Category: Protein-rna complex]]
[[Category: Sm-like motif]]
[[Category: Translation-rna complex]]

Latest revision as of 18:46, 4 October 2023

Crystal structure of YmaH (Hfq) from Bacillus subtilis in complex with an RNA aptamer.Crystal structure of YmaH (Hfq) from Bacillus subtilis in complex with an RNA aptamer.

Structural highlights

3ahu is a 4 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HFQ_BACSU RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.[HAMAP-Rule:MF_00436]

See Also

3ahu, resolution 2.20Å

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