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Literature summary extracted from

  • Wang, T.; Li, H.; Lin, G.; Tang, C.; Li, D.; Nathan, C.; Darwin, K.H.; Li, H.
    Structural insights on the Mycobacterium tuberculosis proteasomal ATPase Mpa (2009), Structure, 17, 1377-1385.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.6.1.5 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

EC Number Protein Variants Comment Organism
5.6.1.5 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.6.1.5 16600
-
 6 * 20000, SDS-PAGE, 6 * 16600, predicted Mycobacterium tuberculosis
5.6.1.5 20000
-
 6 * 20000, SDS-PAGE, 6 * 16600, predicted Mycobacterium tuberculosis
5.6.1.5 100000
-
 gel filtration, suggesting that Mpa-ID oligomerized in solution as a hexamer Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
5.6.1.5 Mycobacterium tuberculosis P9WQN5 Mpa-ID, a 150 amino acid interdomain of Mpa, from Pro97 to Glu245
-
5.6.1.5 Mycobacterium tuberculosis H37Rv P9WQN5 Mpa-ID, a 150 amino acid interdomain of Mpa, from Pro97 to Glu245
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.1.5 full length protein, the interdomain Mpa-ID and the mutant forms Mycobacterium tuberculosis

Subunits

EC Number Subunits Comment Organism
5.6.1.5 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
5.6.1.5 hexamer 6 * 20000, SDS-PAGE, 6 * 16600, predicted Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
5.6.1.5 mpA
-
 Mycobacterium tuberculosis
5.6.1.5 Mtb proteasomal ATPase
-
 Mycobacterium tuberculosis
5.6.1.5 proteasomal ATPase Mpa
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
5.6.1.5 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