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Literature summary for 5.6.1.5 extracted from

  • Sutter, M.; Striebel, F.; Damberger, F.F.; Allain, F.H.; Weber-Ban, E.
    A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa (2009), FEBS Lett., 583, 3151-3157.
    View publication on PubMed

Crystallization (Commentary)

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

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WQN5
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Mycobacterium tuberculosis H37Rv P9WQN5
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Purification (Commentary)

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

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

Synonyms Comment Organism
ARC
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Mycobacterium tuberculosis
mpA
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Mycobacterium tuberculosis
proteasomal ATPase Mpa
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Mycobacterium tuberculosis