Comparative Structural Analysis of Escherichia Coli Cyay at Room and Cryogenic Temperatures Using Macromolecular and Serial Crystallography
Frataxin is a 23 kDa mitochondrial iron-binding protein involved in the biogenesis of iron-sulfur (Fe-S) clusters. Deficiency in frataxin is associated with Friedreich's ataxia, a progressive neurodegenerative disorder. CyaY, the bacterial ortholog of eukaryotic frataxin, is believed to function as an iron donor in Fe-S cluster assembly, making it a key target for structural and functional studies. In this work, a comprehensive structural analysis of the Escherichia coli CyaY protein is presented, comparing its structure at room temperature and cryogenic conditions. Notably, the first room-temperature structures are obtained using the Turkish Light Source "Turkish DeLight" X-ray diffractometer and serial synchrotron X-ray crystallography, marking a significant step forward in understanding CyaY under near-physiological conditions.
Authors
- Nilüfer Baldir (ORCID: https://orcid.org/0000-0002-8829-3287)
- Jongbum Na (ORCID: https://orcid.org/0000-0002-4342-022X)
- Alaleh Shafiei (ORCID: https://orcid.org/0000-0003-2424-9583)
- Hasan DeMi̇rci̇ (ORCID: https://orcid.org/0000-0002-9135-5397)
- Jin Hae Kim (ORCID: https://orcid.org/0000-0002-6776-2451)
Institutions
- Koç University (TR)
- Daegu Gyeongbuk Institute of Science and Technology (KR)
- SLAC National Accelerator Laboratory (US)
Publication Details
- Journal
- ChemBioChem
- Published
- 2025-10-28
- DOI
- https://doi.org/10.1002/cbic.202500442
- Citations
- 1
- Primary Topic
- Metalloenzymes and iron-sulfur proteins
- Type
- article
- Field-Weighted Citation Impact
- 0.36