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Crystal structure of ERA: A GTPase-dependent cell cycle regulator containing an RNA binding motif

  1. Author:
    Chen, X.
    Court, D. L.
    Ji, X. H.

  2. Author Address

    Ji XH NCI, Biomol Struct Grp, Frederick Canc Res & Dev Ctr POB B Ft Detrick, MD 21702 USA NCI, Biomol Struct Grp, Frederick Canc Res & Dev Ctr Ft Detrick, MD 21702 USA NCI, Mol Control & Genet Sect, Adv BioSci Labs,Basic Res Program, Frederick Canc Res & Dev Ctr Ft Detrick, MD 21702 USA
    1. Year: 1999
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 96
    2. 15
    3. Pages: 8396-8401
  4. Type of Article: Article
  1. Abstract:

    ERA forms a unique family of GTPase. It is widely conserved and essential in bacteria. ERI functions in cell cycle control by coupling cell division with growth rate, ERA homologues also are found in eukaryotes. Here we report the crystal structure of ERA from Escherichia coli. The structure has been determined at 2.4-Angstrom resolution. It reveals a tno domain arrangement of the molecule: an N-terminal domain that resembles p21 Ras and a C-terminal domain that is unique. Structure-based topological search of the C domain fails to reveal any meaningful match, although sequence analysis suggests that it contains a KH domain. KH domains are RNA binding motifs that usually occur in tandem repeats and exhibit low sequence similarity except for the well-conserved segment VIGxxGxxIK. We have identified a beta alpha alpha beta fold that contains the VIGxxGxxIK sequence and is shared by the C domain of ERA and the ECH domain. We propose that this beta alpha alpha beta fold is the RNA binding motif, the minimum structural requirement for RNA binding, ERA dimerizes in crystal. The dimer formation involves a significantly distorted switch II region, which may shed light on how ERA protein regulates downstream events. [References: 49]

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