ArticleProtein science : a publication of the Protein Society2003
Atomic resolution analysis of the catalytic site of an aspartic proteinase and an unexpected mode of binding by short peptides.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen Bonds.Biochemistry · 2026Article
- Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen Bonds.bioRxiv : the preprint server for biology · 2025Article
- Room-temperature neutron and X-ray data collection of 3CL MActa crystallographica. Section F, Structural biology communications · 2020Article
- Encapsulation of Aspartic Protease in Nonlamellar Lipid Liquid Crystalline Phases.Biophysical journal · 2019Article
- Short Carboxylic Acid-Carboxylate Hydrogen Bonds Can Have Fully Localized Protons.Biochemistry · 2017Article
- Structural studies of vacuolar plasmepsins.Biochimica et biophysica acta · 2012Review
- Structural insights into the activation and inhibition of histo-aspartic protease from Plasmodium falciparum.Biochemistry · 2011Article
- Crystal structures of the histo-aspartic protease (HAP) from Plasmodium falciparum.Journal of molecular biology · 2009Article
- Cysteine pKa depression by a protonated glutamic acid in human DJ-1.Biochemistry · 2008Article
- X-ray, neutron and NMR studies of the catalytic mechanism of aspartic proteinases.European biophysics journal : EBJ · 2006Article
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7 authors.
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Abstract
The X-ray structures of native endothiapepsin and a complex with a hydroxyethylene transition state analog inhibitor (H261) have been determined at atomic resolution. Unrestrained refinement of the carboxyl groups of the enzyme by using the atomic resolution data indicates that both catalytic aspartates in the native enzyme share a single negative charge equally; that is, in the crystal, one half of the active sites have Asp 32 ionized and the other half have Asp 215 ionized. The electron density map of the native enzyme refined at 0.9 A resolution demonstrates that there is a short peptide (probably Ser-Thr) bound noncovalently in the active site cleft. The N-terminal nitrogen of the dipeptide interacts with the aspartate diad of the enzyme by hydrogen bonds involving the carboxyl of Asp 215 and the catalytic water molecule. This is consistent with classical findings that the aspartic proteinases can be inhibited weakly by short peptides and that these enzymes can catalyze transpeptidation reactions. The dipeptide may originate from autolysis of the N-terminal Ser-Thr sequence of the enzyme during crystallization.
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