Crystallization (Comment) | Organism |
---|---|
characterization of the structural determinants of Pup (mybacterial ubiquitin-like protein) and its interaction witrh Mpa. The N-terminal coiled-coil domain of Mpa makes extensive contacts along the central region (residues 21-58) of Pup leaving its N-terminal uncontrained and available for other functional interactions | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WQN5 | - |
- |
Mycobacterium tuberculosis H37Rv | P9WQN5 | - |
- |
Purification (Comment) | Organism |
---|---|
Mpa fragments are purified as N-terminal fusions with His6-tagged maltose-binding protein followed by a TEV cleavage site, producing the folowing fragments: Mpa-wt (residues 1-609), Mpa-CC (residues 1-98), Mpa-ID (99-216), and Mpa-CC-ID (1-216) | Mycobacterium tuberculosis |
Subunits | Comment | Organism |
---|---|---|
hexamer | Mpa is a monomer of 67000 Da that assembles into a hexameric ring. Each monomer consists of three main regions, an N-terminal coiled-coil domain (CC, residues 1-98), an interdomain (ID, residues 99-216) and an ATPase domain of the AAA-type (residues 217-609). The N-terminal coiled-coil domain of Mpa specifically interacts with Pub-decorated beads, indicating that it mediates the binding to pupylated substrates | Mycobacterium tuberculosis |
monomer | Mpa is a monomer of 67000 Da that assembles into a hexameric ring. Each monomer consists of three main regions, an N-terminal coiled-coil domain (CC, residues 1-98), an interdomain (ID, residues 99-216) and an ATPase domain of the AAA-type (residues 217-609). The N-terminal coiled-coil domain of Mpa specifically interacts with Pub-decorated beads, indicating that it mediates the binding to pupylated substrates | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
ARC | - |
Mycobacterium tuberculosis |
mpA | - |
Mycobacterium tuberculosis |
proteasomal ATPase Mpa | - |
Mycobacterium tuberculosis |