Singh Chingakham R, Lovell Scott, Mehzabeen Nurjahan, Chowdhury Wasimul Q, Geanes Eric S, Battaile Kevin P, Roelofs Jeroen
Division of Biology, Kansas State University, 338 Ackert Hall, Manhattan, KS 66506, USA.
Protein Structure Laboratory, University of Kansas, Del Shankel Structural Biology Center, Lawrence, KS 66047, USA.
Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):418-23. doi: 10.1107/S2053230X14003884. Epub 2014 Mar 25.
The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-terminus of Rpt5 for binding. Here, the 1.15 Å resolution structure of the PDZ domain of Nas2 is reported. This structure will provide a basis for further insights regarding the structure and function of Nas2 in proteasome assembly.
26S蛋白酶体是一种2.5兆道尔顿的蛋白酶,专门负责真核生物中泛素化蛋白的降解。这种包含66种多肽的复合物的组装由至少九种蛋白酶体特异性伴侣蛋白协助。其中之一Nas2与蛋白酶体的AAA - ATP酶亚基Rpt5结合。Nas2的PDZ结构域与Rpt5的C末端尾巴结合;然而,它结合Rpt5并不需要Rpt5的C末端。在此,报道了Nas2的PDZ结构域分辨率为1.15埃的结构。该结构将为进一步深入了解Nas2在蛋白酶体组装中的结构和功能提供基础。