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PMID: 10411886 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 96 ·No. 15 ·1999-07-20 ·Pages 8396-401

Chen X, Court DL, Ji X

Abstract

ERA forms a unique family of GTPase. It is widely conserved and essential in bacteria. ERA 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-A resolution. It reveals a two-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 betaalphaalphabeta fold that contains the VIGxxGxxIK sequence and is shared by the C domain of ERA and the KH domain. We propose that this betaalphaalphabeta 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.

MeSH Terms
Bacterial Proteins/chemistry Binding Sites Cell Cycle Crystallography, X-Ray Dimerization Escherichia coli/chemistry Escherichia coli Proteins Fragile X Mental Retardation Protein GTP Phosphohydrolases/chemistry GTP-Binding Proteins/chemistry Hydrogen Bonding Membrane Proteins/chemistry Models, Molecular Nerve Tissue Proteins Protein Folding Protein Structure, Secondary RNA-Binding Proteins/chemistry ras Proteins/chemistry
Chemicals
Bacterial Proteins Escherichia coli Proteins Membrane Proteins Nerve Tissue Proteins RNA-Binding Proteins era protein, E coli Fragile X Mental Retardation Protein GTP Phosphohydrolases GTP-Binding Proteins ras Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Chen X
Biomolecular Structure Group, Advanced BioScience Laboratories-Basic Research Program, National Cancer Institute-Frederick Cancer Research and Development Center, P.O. Box B, Frederick, MD 21702, USA.
Court D L
Ji X
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.96.15.8396
Published
1999-07-20
Pages
8396-401
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC17527
Subset
IM
Databases
PDB
1EGA
External Links
PubMed source DOI: 10.1073/pnas.96.15.8396 PMC Full Text View journal details
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