ArticleProtein science : a publication of the Protein Society2005
Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 56 citations in OpenAlex.
- Structural evidence of thioacetate reduction by fluorescent protein mRuby.European biophysics journal : EBJ · 2026Article
- Mapping the effects of specific radiation damage and solvent radiolysis in buffers and crystals with online UV-Vis absorption spectroscopy.Acta crystallographica. Section D, Structural biology · 2026Article
- Molecular Basis of Interchain Disulfide Bond Formation in BMP-9 and BMP-10.Journal of molecular biology · 2025Article
- Molecular basis of interchain disulfide-bond formation in BMP-9 and BMP-10.bioRxiv : the preprint server for biology · 2024Article
- Identifying and avoiding radiation damage in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024Article
- Structure of mycobacterial ergothioneine-biosynthesis C-S lyase EgtE.The Journal of biological chemistry · 2024Article
- L-serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase.Protein science : a publication of the Protein Society · 2023Article
- Molecular Structure of Phosphoserine Aminotransferase fromInternational journal of molecular sciences · 2023Article
- Quantifying and comparing radiation damage in the Protein Data Bank.Nature communications · 2022Article
- The Effects of Ionising and Non-Ionising Electromagnetic Radiation on Extracellular Matrix Proteins.Cells · 2021Review
- Article
- Radiation damage at the active site of human alanine:glyoxylate aminotransferase reveals that the cofactor position is finely tuned during catalysis.Scientific reports · 2017Article
- Lysine relay mechanism coordinates intermediate transfer in vitamin B6 biosynthesis.Nature chemical biology · 2017Article
- OH cleavage from tyrosine: debunking a myth.Journal of synchrotron radiation · 2017Article
- RNA protects a nucleoprotein complex against radiation damage.Acta crystallographica. Section D, Structural biology · 2016Article
- In crystallo optical spectroscopy (icOS) as a complementary tool on the macromolecular crystallography beamlines of the ESRF.Acta crystallographica. Section D, Biological crystallography · 2015Article
- A survey of global radiation damage to 15 different protein crystal types at room temperature: a new decay model.Journal of synchrotron radiation · 2013Article
- Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with α-ketoisocaproate and L-glutamate suggest the radiation resistance of this enzyme for catalysis.Journal of bacteriology · 2012Article
- The kinetic dose limit in room-temperature time-resolved macromolecular crystallography.Journal of synchrotron radiation · 2012Article
- Radiation damage in macromolecular crystallography: what is it and why should we care?Acta crystallographica. Section D, Biological crystallography · 2010Article
Corrections and comments
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Authors and funding
4 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The X-ray susceptibility of the lysine-pyridoxal-5'-phosphate Schiff base in Bacillus alcalophilus phosphoserine aminotransferase has been investigated using crystallographic data collected at 100 K to 1.3 A resolution, complemented by on-line spectroscopic studies. X-rays induce deprotonation of the internal aldimine, changes in the Schiff base conformation, displacement of the cofactor molecule, and disruption of the Schiff base linkage between pyridoxal-5'-phosphate and the Lys residue. Analysis of the "undamaged" structure reveals a significant chemical strain on the internal aldimine bond that leads to a pronounced geometrical distortion of the cofactor. However, upon crystal exposure to the X-rays, the strain and distortion are relaxed and eventually diminished when the total absorbed dose has exceeded 4.7 x 10(6) Ggamma. Our data provide new insights into the enzymatic activation of pyridoxal-5'-phosphate and suggest that special care should be taken while using macromolecular crystallography to study details in strained active sites.
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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.