proteindiffraction

proteindiffraction provides access to high-resolution X-ray crystallography diffraction images and linked Protein Data Bank (PDB) coordinates and structure factors to support determination and analysis of protein structures, including enzyme mechanism and antibiotic-target studies.

Key Features:

• Access to high-resolution diffraction images: Direct access to X-ray crystallography diffraction images for diverse protein structures to enable independent analyses and validation of structural data.
• Integration with structural databases: Linked to the Protein Data Bank (PDB) to retrieve coordinates and structure factors associated with specific PDB accession numbers.
• BaPDH complex datasets: Provides ternary and binary complex structures of Bacillus anthracis prephenate dehydrogenase (BaPDH) with NAD+ and tyrosine and isolated ACT domain dimer structures.
• Metadata and provenance: Supplies associated metadata such as DOIs for diffraction images and datasets.
• Source experimental data: Hosts raw diffraction images obtained from X-ray crystallography experiments for atomic structure determination.

Scientific Applications:

• Enzyme mechanism elucidation: Enables study of the unique allosteric inhibition of BaPDH by tyrosine via the ACT domain, contrasting with competitive inhibition in other prephenate dehydrogenases.
• Structural analysis and drug design: Supports rational inhibitor design by providing structural data on BaPDH complexes with NAD+ and tyrosine and isolated ACT domain dimers.
• Pathogen-specific enzyme inhibition studies: Facilitates investigation of inhibition strategies for enzymes from antibiotic-resistant pathogens listed by the World Health Organization.

Methodology:

Uses diffraction images obtained from X-ray crystallography experiments for atomic structure determination and provides associated metadata such as DOIs.