Crystallization and preliminary X-ray crystallographic analysis of the N domain of p97/VCP in complex with the UBX domain of FAF1
| Autor: | Hwa Young Shin, Sang Yoon Lee, Wonchull Kang, Jin Kuk Yang |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Valosin-containing protein
Biophysics Cell Cycle Proteins Crystallography X-Ray Biochemistry Protein structure Ubiquitin Valosin Containing Protein Structural Biology Genetics Humans Cell Cycle Protein Ultrabithorax Adaptor Proteins Signal Transducing Adenosine Triphosphatases biology Chemistry Signal transducing adaptor protein Condensed Matter Physics Protein Structure Tertiary Crystallography Proteasome Crystallization Communications Chaperone (protein) biology.protein Apoptosis Regulatory Proteins Crystallization |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:41-43 |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309109047691 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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