ArticlePloS one2011
The initiation of GTP hydrolysis by the G-domain of FeoB: insights from a transition-state complex structure.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- The structure of the full catalytic cycle ofbioRxiv : the preprint server for biology · 2025Article
- Characterization of intact FeoB in a lipid bilayer using styrene-maleic acid (SMA) copolymers.Biochimica et biophysica acta. Biomembranes · 2025Article
- Iron Homeostasis inBiology · 2023Review
- Structures and coordination chemistry of transporters involved in manganese and iron homeostasis.Biochemical Society transactions · 2023Review
- The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes.Metallomics : integrated biometal science · 2022Review
- Structural basis of elongation factor 2 switching.Current research in structural biology · 2020Article
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- Article
- Identification of anti-Gram-negative bacteria agents targeting the interaction between ribosomal proteins L12 and L10.Acta pharmaceutica Sinica. B · 2018Article
- The GTPase hGBP1 converts GTP to GMP in two stepsChemical science · 2017Article
- Vibrio cholerae FeoA, FeoB, and FeoC Interact To Form a Complex.Journal of bacteriology · 2016Article
- Structural model of FeoB, the iron transporter from Pseudomonas aeruginosa, predicts a cysteine lined, GTP-gated pore.Bioscience reports · 2016Article
- Histidine 114 Is Critical for ATP Hydrolysis by the Universally Conserved ATPase YchF.The Journal of biological chemistry · 2015Article
- A monovalent cation acts as structural and catalytic cofactor in translational GTPases.The EMBO journal · 2014Article
- FeoA and FeoC are essential components of the Vibrio cholerae ferrous iron uptake system, and FeoC interacts with FeoB.Journal of bacteriology · 2013Article
- Evolution of the genetic code by incorporation of amino acids that improved or changed protein function.Journal of molecular evolution · 2013Article
- Mutational analysis of the ribosome assembly GTPase RbgA provides insight into ribosome interaction and ribosome-stimulated GTPase activation.Nucleic acids research · 2013Article
- Crystal structure of the Klebsiella pneumoniae NFeoB/FeoC complex and roles of FeoC in regulation of Fe2+ transport by the bacterial Feo system.Journal of bacteriology · 2012Article
- Biochemical characterization of ribosome assembly GTPase RbgA in Bacillus subtilis.The Journal of biological chemistry · 2012Article
- Potassium acts as a GTPase-activating element on each nucleotide-binding domain of the essential Bacillus subtilis EngA.PloS one · 2012Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The polytopic membrane protein FeoB is a ferrous iron transporter in prokaryotes. The protein contains a potassium-activated GTPase domain that is essential in regulating the import of iron and conferring virulence to many disease-causing bacteria. However, the mechanism by which the G-domain of FeoB hydrolyzes GTP is not well understood. In particular, it is not yet known how the pivotal step in GTP hydrolysis is achieved: alignment of a catalytic water molecule. In the current study, the crystal structure of the soluble domains from Streptococcus thermophilus FeoB (NFeoB(St)) in complex with the activating potassium ion and a transition-state analogue, GDP⋅AlF(4) (-), reveals a novel mode of water alignment involving contacts with the protein backbone only. In parallel to the structural studies, a series of seven mutant proteins were constructed that targeted conserved residues at the active site of NFeoB(St), and the nucleotide binding and hydrolysis properties of these were measured and compared to the wild-type protein. The results show that mutations in Thr35 abolish GTPase activity of the protein, while other conserved residues (Tyr58, Ser64, Glu66 and Glu67) are not required for water alignment by NFeoB(St). Together with the crystal structure, the findings suggest a new mechanism for hydrolysis initiation in small G-proteins, in which the attacking water molecule is aligned by contacts with the protein backbone only.
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