Crystallization (Comment) | Organism |
---|---|
of the conserved interdomain shows a five stranded double beta barrel structure containing a Greek key motif, 2.0 A resolution. Structure and mutational analysis indicate a major role of the interdomain for Mpa hexamerization. The central in the Mpa hexamer is involved in protein substrate translocation and degradation. Mpa is a multidomain structure, with an N-terminal coiled coil domain, a 150 amino acid interdomain (Mpa-ID) that is unique to the proteasome-associated ATPases, a canonical AAA (ATPase associated with various activities) domain, and a small C-terminal domain. The Mpa-ID forms a tightly packed ring-shaped hexamer in the crystal structure as well as in solution. In fact, two hexamers stack end to end, forming a dodecamer, being the packiung unit in the crystal structure | Mycobacterium tuberculosis |
Protein Variants | Comment | Organism |
---|---|---|
R173E/W187A/K235E | triple mutant disrupts the salt-bridges and the hydrophobic interaction during hexamerization. In gel filtration the triple mutant Mpa-ID elutes as monomeric | Mycobacterium tuberculosis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
16600 | - |
6 * 20000, SDS-PAGE, 6 * 16600, predicted | Mycobacterium tuberculosis |
20000 | - |
6 * 20000, SDS-PAGE, 6 * 16600, predicted | Mycobacterium tuberculosis |
100000 | - |
gel filtration, suggesting that Mpa-ID oligomerized in solution as a hexamer | Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WQN5 | Mpa-ID, a 150 amino acid interdomain of Mpa, from Pro97 to Glu245 | - |
Mycobacterium tuberculosis H37Rv | P9WQN5 | Mpa-ID, a 150 amino acid interdomain of Mpa, from Pro97 to Glu245 | - |
Purification (Comment) | Organism |
---|---|
full length protein, the interdomain Mpa-ID and the mutant forms | Mycobacterium tuberculosis |
Subunits | Comment | Organism |
---|---|---|
dodecamer | Mpa-ID forms hexamers in the crystal structure, two hexamers stack end to end, forming a dodecamer, being the packing unit in the crystal structure | Mycobacterium tuberculosis |
hexamer | 6 * 20000, SDS-PAGE, 6 * 16600, predicted | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
mpA | - |
Mycobacterium tuberculosis |
Mtb proteasomal ATPase | - |
Mycobacterium tuberculosis |
proteasomal ATPase Mpa | - |
Mycobacterium tuberculosis |
General Information | Comment | Organism |
---|---|---|
physiological function | proteasome-mediated protein turnover in all domains of life is an energy-dependent process that requires ATPase activity. Mycobacterium tuberculosis possesses an ubiquitin-like proteasome pathway that plays an essential role in its resistance to killing by products of host macrophages | Mycobacterium tuberculosis |