Protein Hfq: Difference between revisions

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== Structural highlights ==
== Structural highlights ==


The biological assembly of Protein Hfq from ''E. coli'' is <scene name='87/875687/Cv/2'>homohexamer</scene> (PDB code [[4ht9]]). The 3D structure of the complex between Hfq and <scene name='87/875687/Cv/5'>poly(A) RNA and poly(U) RNA</scene> shows the poly(A) binding at the distal face of Hfq and poly(U) binding at its proximal face. For the poly(A) A-R-N binding site the A site shows <scene name='87/875687/Cv/4'>hydrogen bonding to Gln and Lys</scene>.  The <scene name='87/875687/Cv/6'>R site shows stacking interactions as well as hydrogen bonding</scene>. The N site does not show any interaction. The poly(U) binding site of Hfq is a classical uridine binding pocket with both stacking and hydrogen bonding interactions<ref>PMID:23605038</ref>.
The biological assembly of Protein Hfq from ''E. coli'' is <scene name='87/875687/Cv/2'>homohexamer</scene> (PDB code [[4ht9]]). The 3D structure of the complex between Hfq and <scene name='87/875687/Cv/5'>poly(A) RNA and poly(U) RNA</scene> shows the poly(A) binding at the distal face of Hfq and poly(U) binding at its proximal face. For the poly(A) A-R-N binding site the A site shows <scene name='87/875687/Cv/4'>hydrogen bonding to Gln and Lys</scene>.  The <scene name='87/875687/Cv/6'>R site shows stacking interactions as well as hydrogen bonding</scene>. The N site does not show any interaction. <scene name='87/875687/Cv/7'>The poly(U) binding site of Hfq is a classical uridine binding pocket with both stacking and hydrogen bonding interactions</scene><ref>PMID:23605038</ref>.
 
</StructureSection>


== 3D Structures of protein Hfq ==
== 3D Structures of protein Hfq ==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[Protein Hfq 3D structures]]
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Protein Hfq
 
**[[1hk9]], [[2y90]], [[2yht]], [[3qhs]], [[4rcb]], [[4rcc]], [[6bdg]] – EcHfq  –  ''Escherichia coli'' <br />
**[[4jli]], [[4jri]], [[4jrk]], [[4juv]] – EcHfq  (mutant)<br />
**[[1u1s]], [[1u1t]], [[4j6y]], [[6xyj]] – PaHfq  –  ''Pseudomonas aeruginosa''<br />
**[[3inz]], [[3m4g]], [[4mml]], [[4mmk]], [[5i21]] – PaHfq  (mutant)<br />
**[[2ylb]] – StHfq  –  ''Salmonella typhimurium''<br />
**[[6gwk]] – Hfq  –  ''Caulobacter crescentus''<br />
**[[4nl2]] – LmHfq – ''Listeria monocytogenes''<br />
**[[4noy]] – LmHfq  (mutant)<br />
**[[5szd]] – AaHfq – ''Aquifex aeolicus''<br />
**[[3sb2]] – Hfq  - ''Herbaspirillum seropedicae''<br />
**[[1kq1]] – SaHfq – ''Staphylococcus aureus''<br />
**[[2qtx]], [[4x9c]] – MjHfq – ''Methanococcus jannaschii''<br />
**[[3hfn]] – Hfq  - ''Anabaena''<br />
 
*Protein Hfq complex with nucleotide
 
**[[3res]] – EcHfq  + ADP<br />
**[[3qo3]] – EcHfq  + ATP<br />
**[[4pno]] – EcHfq  + UMP<br />
**[[4j6x]] – PaHfq  + UTP<br />
**[[3qui]] – PaHfq  + ADPNP<br />
**[[4j5y]] – PaHfq  + ATP<br />
**[[4j6w]] – PaHfq  + CTP<br />
**[[2ylc]] – StHfq  + UMP<br />
**[[5dy9]] – MjHfq  (mutant) + AMP<br />
**[[4x9d]] – MjHfq + UMP<br />
 
*Protein Hfq other complexes
 
**[[6qlb]] – EcHfq + calpain <br />
**[[3vu3]] – EcHfq + catalase <br />
**[[3gib]], [[4ht8]] – EcHfq + poly(A)<br />
**[[4ht9]], [[5new]] – EcHfq + poly(A) + poly(U)<br />
**[[3rer]] – EcHfq + poly(U) + ADP<br />
**[[4qvc]], [[4qvd]] – EcHfq + RNA<br />
**[[5uk7]] – EcHfq + DNA<br />
**[[3ahu]], [[3hsb]] – Hfq + RNA  –  ''Bacillus subtilis''<br />
**[[6o1k]], [[6o1l]], [[6o1m]] – PaHfq  + Crc + RNA – Cryo EM<br />
**[[4v2s]] – StHfq + sRNA<br />
**[[4y91]] – Hfq + poly(U) – ''Thermotoga maritima''<br />
**[[4nl3]] – LmHfq + poly(U) <br />
**[[5sze]] – AaHfq + poly(U) <br />
**[[1kq2]] – SaHfq + RNA <br />
}}
 


== References ==
== References ==
<references/>
<references/>
 
</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 13:18, 14 September 2023


Function

Protein Hfq (Hfq) (Host Factor for Qβ) or RNA-binding protein Hfq is stimulating base-pairing between sRNA and target mRNA by binding both RNAs via three RNA-binding surfaces. Hfq is found in enteric bacteria[1]. Hfq binds RNA via poly(A-R-N) triplets where A is adenosine, R is purine nucleotide and N is any nucleotide[2].

Relevance

Since Hfq is required for gene regulation and infectivity of some Gram-negative bacteria its mutations can eliminate infectivity of Lyme disease caused by the bacteria Borellia burgdorferi, for example[3].

Structural highlights

The biological assembly of Protein Hfq from E. coli is (PDB code 4ht9). The 3D structure of the complex between Hfq and shows the poly(A) binding at the distal face of Hfq and poly(U) binding at its proximal face. For the poly(A) A-R-N binding site the A site shows . The . The N site does not show any interaction. [4].

3D Structures of protein Hfq

Protein Hfq 3D structures

References

  1. ↑ Morita T, Aiba H. Mechanism and physiological significance of autoregulation of the Escherichia coli hfq gene. RNA. 2019 Feb;25(2):264-276. doi: 10.1261/rna.068106.118. Epub 2018 Nov 28. PMID:30487269 doi:http://dx.doi.org/10.1261/rna.068106.118
  2. ↑ Link TM, Valentin-Hansen P, Brennan RG. Structure of Escherichia coli Hfq bound to polyriboadenylate RNA. Proc Natl Acad Sci U S A. 2009 Nov 4. PMID:19889981
  3. ↑ Lybecker MC, Abel CA, Feig AL, Samuels DS. Identification and function of the RNA chaperone Hfq in the Lyme disease spirochete Borrelia burgdorferi. Mol Microbiol. 2010 Nov;78(3):622-35. doi: 10.1111/j.1365-2958.2010.07374.x. Epub, 2010 Sep 27. PMID:20815822 doi:http://dx.doi.org/10.1111/j.1365-2958.2010.07374.x
  4. ↑ Wang W, Wang L, Wu J, Gong Q, Shi Y. Hfq-bridged ternary complex is important for translation activation of rpoS by DsrA. Nucleic Acids Res. 2013 Jun 1;41(11):5938-48. doi: 10.1093/nar/gkt276. Epub 2013 , Apr 19. PMID:23605038 doi:10.1093/nar/gkt276

Structure of E. coli hexameric Hfq complex with poly(A) RNA and poly(U) RNA (PDB code 4ht9)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky
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