9V63

Crystal structure of Escherichia coli CyaY by fixed target serial synchrotron crystallography

Summary for 9V63

• Entry DOI: 10.2210/pdb9v63/pdb
• Descriptor: Iron-sulfur cluster assembly protein CyaY (2 entities in total)
• Functional Keywords: cyay, escherichia coli, frataxin, metal binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 12242.36

Authors

Shafiei, A.,DeMirci, H. (deposition date: 2025-05-26, release date: 2026-05-06)

Primary citation

Shafiei, A.,Baldir, N.,Na, J.,Kim, J.H.,DeMirci, H.
Comparative Structural Analysis of Escherichia Coli Cyay at Room and Cryogenic Temperatures Using Macromolecular and Serial Crystallography.
Chembiochem, 26:e202500442-e202500442, 2025

PubMed Abstract: 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.

PubMed: 41147201
DOI: 10.1002/cbic.202500442

Experimental method

X-RAY DIFFRACTION (1.7 Å)