4J6W: Crystal Structure Of Hfq From Pseudomonas Aeruginosa In Complex With Ctp

Citation:
Acta Crystallogr. D Biol. Crystallogr. (2013) 69 p.1504-1513
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.
PDB ID: 4J6WDownload
MMDB ID: 112245
PDB Deposition Date: 2013/2/12
Updated in MMDB: 2013/08
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 4J6W: hexameric; determined by author and by software (PISA)
Molecular Components in 4J6W
Label Count Molecule
Proteins (6 molecules)
6
Protein HFQ(Gene symbol: hfq)
Molecule annotation
Chemicals (25 molecules)
1
6
2
4
3
8
4
3
5
1
6
2
7
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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