Literature summary for 5.6.1.5 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.

Crystallization (Commentary)

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

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

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 [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

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 (Commentary)

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

Subunits

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

Synonyms	Comment	Organism
mpA	-	Mycobacterium tuberculosis
Mtb proteasomal ATPase	-	Mycobacterium tuberculosis
proteasomal ATPase Mpa	-	Mycobacterium tuberculosis

General Information

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