1m7c

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

STUCTURAL MODEL OF E. COLI HFQ

spinqualitylabelsall models 1m7c Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed The Hfq polypeptide of Escherichia coli is a nucleic acid-binding protein involved in the expression of many proteins. Derivation of its three-dimensional structure is important for our understanding of its role in gene regulation at the molecular level. In this study, we combined computational and biophysical analysis to derive a possible structure for Hfq. As a first step towards determining the structure, we searched for possible sequence-structure compatibility, using secondary structure prediction and protein domain and fold-recognition methods available on the WEB. One fold, essentially beta sheet in character, the Sm motif of small nuclear ribonucleoproteins, even though it initially fell well below the confidence thresholds, was proposed and further validated by a series of biophysical and biochemical studies. The Hfq hexamer structure was modelled on the human Sm D3B structure using optimised sequence alignments and molecular mechanics methods. This structure accounts for the physico-chemical properties of Hfq and highlights amino acid residues that could interact with RNA. Structural Modelling of the Sm-like Protein Hfq from Escherichia coli.,Arluison V, Derreumaux P, Allemand F, Folichon M, Hajnsdorf E, Regnier P J Mol Biol. 2002 Jul 19;320(4):705-12. PMID:12095248 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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