EC Number   |
|---|
   5.6.1.5 | - |
| 5.6.1.5 | apo and ADP-bound enzyme forms, sitting or hanging drop vapor diffusion methods, using 0.1 M Tris-HCl, pH 8.2, 20% (w/v) PEG 400, 0.2M MgCl2 or 100 mM Bis-Tris propane, pH 7.0, 0.475 M NaCl, 18.2% (w/v) PEG 4000 |
| 5.6.1.5 | 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 |
| 5.6.1.5 | crystal structure of the archaeal 20S proteasome in complex with the C-terminus of the archaeal proteasome regulatory ATPase, PAN is determined. This structure defines the detailed interactions between the critical C-terminal HbYX motif and the 20S a-subunits and indicates that the intersubunit pocket in the 20S undergoes an induced-fit conformational change on binding of the HbYX motif |
| 5.6.1.5 | crystal structures of full-length Hsm3 and the complex with the C-terminal domain of Rpt1 is determined |
| 5.6.1.5 | eukaryotic ATPases form a heterohexameric ring with the arrangement Rpt1-Rpt2-Rpt6-Rpt3-Rpt4-Rpt5 (Rp, regulatory particles) in fully assembled proteasomes. This quaternary organization clarifies the functional overlap of specific RP assembly chaperones and leads to the identification of a potential RP assembly intermediate that includes four ATPases (Rpt6-Rpt3-Rpt4-Rpt5) and their cognate chaperones Rpn14, Nas6, and Nas2 |
| 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 |
| 5.6.1.5 | purified recombinant N-terminus of p27 (residues 1-128) in complex with the C-terminal ATPase domain of Rpt5 (residues 173-442), sitting drop method, mixing of 0.001 ml of 4 mg/ml protein in 10 mM HEPES pH 7.5, 50 mM NaCl, 1 mM EDTA, 1 mM DTT, with 0.001 ml of precipitant solution containing 2.0 M NaCl, 10% PEG 6000, X-ray diffraction structure determination and analysis at 1.7 A and 4.0 A resolution, respectively |
| 5.6.1.5 | structure solved by multiple isomorphous replacement. One ARC-N monomer consists of two oligosaccharide-binding domains in tandem, the first from Ser80 to Tyr136 (OB1) and the second from Gly140 to Lys217 (OB2). The domains associate separately into hexameric rings |
| 5.6.1.5 | the structure is solved by molecular replacement with the N-terminal actinobacterial proteasomal ATPase oligosaccharide-binding domain OB1 as the search model. Each PAN-N monomer consists of an N-terminal coiled-coil helix and a C-terminal OB domain. The helices form two-strands coiled coils, while the OB domains associate into hexameric rings. Thus the structure can be described as a trimer of dimers |
