ArticleProceedings of the National Academy of Sciences of the United States of America1999
Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 104 citations in OpenAlex.
- Population Ecology of Glacier Bacteria from the View of Gene Flow inMicroorganisms · 2026Article
- Nucleic acid-binding KH domain proteins influence a spectrum of biological pathways including as part of membrane-localized complexes.Journal of structural biology: X · 2024Article
- A simple, robust, broadly applicable insertion mutagenesis method to create random fluorescent protein: target protein fusions.G3 (Bethesda, Md.) · 2024Article
- GTPase Era at the heart of ribosome assembly.Frontiers in molecular biosciences · 2023Review
- Protein Assistants of Small Ribosomal Subunit Biogenesis in Bacteria.Microorganisms · 2022Review
- Role of Era in assembly and homeostasis of the ribosomal small subunit.Nucleic acids research · 2019Article
- WSL6 encoding an Era-type GTP-binding protein is essential for chloroplast development in rice.Plant molecular biology · 2019Article
- The (p)ppGpp-binding GTPase Era promotes rRNA processing and cold adaptation in Staphylococcus aureus.PLoS genetics · 2019Article
- Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases.PLoS biology · 2019Article
- Crystal structure of a putative quorum sensing-regulated protein (PA3611) from the Pseudomonas-specific DUF4146 family.Proteins · 2014Article
- DER containing two consecutive GTP-binding domains plays an essential role in chloroplast ribosomal RNA processing and ribosome biogenesis in higher plants.Journal of experimental botany · 2014Article
- RNase III: Genetics and function; structure and mechanism.Annual review of genetics · 2013Review
- The universally conserved prokaryotic GTPases.Microbiology and molecular biology reviews : MMBR · 2011Review
- Effects of site-directed mutagenesis of mglA on motility and swarming of Myxococcus xanthus.BMC microbiology · 2010Article
- Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB.Journal of structural biology · 2010Article
- The effect of ribosome assembly cofactors on in vitro 30S subunit reconstitution.Journal of molecular biology · 2010Article
- Interaction of an essential Escherichia coli GTPase, Der, with the 50S ribosome via the KH-like domain.Journal of bacteriology · 2010Article
- Structure of ERA in complex with the 3' end of 16S rRNA: implications for ribosome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Crystallization and preliminary X-ray diffraction analysis of the truncated cytosolic domain of the iron transporter FeoB.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Inhibition of bacterial ribosome assembly: a suitable drug target?Microbiology and molecular biology reviews : MMBR · 2009Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.