4J6X

Crystal structure of Hfq from Pseudomonas aeruginosa in complex with UTP

Summary for 4J6X

• Entry DOI: 10.2210/pdb4j6x/pdb
• Related: 1U1S 1U1T 3QUI 4J5Y 4J6W 4J6Y
• Descriptor: Protein hfq, URIDINE 5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: lsm, rna binding protein, rna chaperone, srna, mrna
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 6
• Total formula weight: 57591.77

Authors

Nikulin, A.D.,Murina, V.,Lekontseva, N. (deposition date: 2013-02-12, release date: 2013-07-31, Last modification date: 2023-09-20)

Primary citation

Murina, V.,Lekontseva, N.,Nikulin, A.
Hfq binds ribonucleotides in three different RNA-binding sites.
Acta Crystallogr.,Sect.D, 69:1504-1513, 2013

PubMed Abstract: The Hfq protein forms a doughnut-shaped homohexamer that possesses RNA-binding activity. There are two distinct RNA-binding surfaces located on the proximal and the distal sides of the hexamer. The proximal side is involved in the binding of mRNA and small noncoding RNAs (sRNAs), while the distal side has an affinity for A-rich RNA sequences. In this work, the ability of various ribonucleotides to form complexes with Hfq from Pseudomonas aeruginosa has been tested using X-ray crystallography. ATP and ADPNP have been located in the distal R-site, which is a site for poly(A) RNA binding. UTP has been found in the so-called lateral RNA-binding site at the proximal surface. CTP has been found in both the distal R-site and the proximal U-binding site. GTP did not form a complex with Hfq under the conditions tested. The results have demonstrated the power of the crystallographic method for locating ribonucleotides and predicting single-stranded RNA-binding sites on the protein surface.

PubMed: 23897473
DOI: 10.1107/S090744491301010X

Experimental method

X-RAY DIFFRACTION (2.222 Å)