Crystal structure of the programmed cell death 5 protein from Sulfolobus solfataricus. Issue 2 (4th February 2019)

• Record Type: Journal Article
• Authors: Lin, Kuan-Fu; Hsu, Jia-Yuan; Hsieh, Dong-Lin; Tsai, Meng-Ju; Yeh, Ching-Hui; Chen, Chin-Yu
• Is Part Of: Acta crystallographica. Volume 75:Issue 2(2019:Feb.)
• Page Start: 73
• Page End: 79
• Publication Date: 2019-02-04
• Subjects: Sulfolobus solfataricus -- DNA‐binding protein -- programmed cell death -- X‐ray crystallography -- PDCDS; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X18017673
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The crystal structure of Sso0352 from Sulfolobus solfataricus, a homolog of programmed cell death 5 (PDCD5), was solved using single‐wavelength anomalous diffraction. This is the first crystal structure of a PDCD5 homolog to be solved. Abstract : Programmed cell death 5 (PDCD5) is a vital signaling protein in the apoptosis pathway in eukaryotes. It is known that there are two dissociated N‐terminal regions and a triple‐helix core in eukaryotic PDCD5. Structural and functional studies of PDCD5 from hyperthermophilic archaea have been limited to date. Here, the PDCD5 homolog Sso0352 (SsoPDCD5) was identified in Sulfolobus solfataricus, the SsoPDCD5 protein was expressed and crystallized, and the phase was identified by single‐wavelength anomalous diffraction. The native SsoPDCD5 crystal belonged to space group C 2 and diffracted to 1.49 Å resolution. This is the first crystal structure of a PDCD5 homolog to be solved. SsoPDCD5 shares a similar triple‐helix bundle with eukaryotic PDCD5 but has a long α‐helix in the N‐terminus. A structural search and biochemical data suggest that SsoPDCD5 may function as a DNA‐binding protein.