Protein Hfq: Difference between revisions

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

Michal Harel, Alexander Berchansky

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 == Function ==
-'''Protein Hfq''' (Hfq) ('''H'''ost '''F'''actor for '''Q'''β) 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<ref>PMID:30487269</ref>.  SAP binds in a calcium-dependent fashion to a variety of ligands.
+'''Protein Hfq''' (Hfq) ('''H'''ost '''F'''actor for '''Q'''β) 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<ref>PMID:30487269</ref>.  Hfq binds RNA via poly(A-R-N) triplets where A is adenosine, R is purine nucleotide and N is any nucleotide<ref>PMID:19889981</ref>.
 == Relevance ==
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 == Structural highlights ==
-<scene name='87/875651/Cv/5'>The 3D structure of a complex of SAP with the small molecule ligand AMP</scene> shows the nucleotide phosphate group bridging two Ca+2 ions and forming hydrogen bonds to Asn, Gln and Try residues of SAP  <ref>PMID:9217261</ref>.
+The 3D structure of the complex between Hfq and poly(A) RNA and poly(U) RNA shows the poly(A) binding at the distal tase of Hfq and poly(U) binding at its proximal face.  In the poly(A) A-R-N binding site the A site shows hydrogen bonding to Gln and Lys.  The R site site shows stacking interactions as well as hydrogen bonding.  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>.
 </StructureSection>