Crystallization and preliminary X-ray crystallographic analysis of the N domain of p97/VCP in complex with the UBX domain of FAF1.

Department of Chemistry, College of Natural Sciences, Soongsil University, Seoul 156-743, Republic of Korea.
p97/VCP is a multifunctional AAA(+)-family ATPase that is involved in diverse cellular processes. p97/VCP directly interacts with various adaptors for activity in different biochemical contexts. Among these adaptors are p47 and Fas-associated factor 1 (FAF1), which contain a common UBX domain through which they bind to the N domain of p97/VCP. In the ubiquitin-proteasome pathway, p97/VCP acts as a chaperone that presents client proteins to the proteasome for degradation, while FAF1 modulates the process by interacting with ubiquitinated client proteins and also with p97/VCP. In an effort to elucidate the structural details of the interaction between p97/VCP and FAF1, the p97/VCP N domain was crystallized in complex with the FAF1 UBX domain. X-ray data were collected to 2.60 A resolution and the crystals belonged to space group C222(1), with unit-cell parameters a = 58.24, b = 72.81, c = 132.93 A. The Matthews coefficient and solvent content were estimated to be 2.39 A(3) Da(-1) and 48.4%, respectively, assuming that the asymmetric unit contained p97/VCP N domain and FAF1 molecules in a 1:1 ratio, which was subsequently confirmed by molecular-replacement calculations.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Adenosine Triphosphatases, Cell Cycle Proteins, Crystallization, Crystallography, X-Ray, Humans, Protein Structure, Tertiary
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. Jan. 01, 2010; 66(0);41-3 [PUBMED:20057067]
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