9V63 image
Deposition Date 2025-05-26
Release Date 2026-05-06
Last Version Date 2026-05-06
Entry Detail
PDB ID:
9V63
Title:
Crystal structure of Escherichia coli CyaY by fixed target serial synchrotron crystallography
Biological Source:
Source Organism(s):
Escherichia coli (Taxon ID: 562)
Expression System(s):
Method Details:
Experimental Method:
Resolution:
1.70 Å
R-Value Free:
0.31
R-Value Work:
0.25
Space Group:
P 32 2 1
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Iron-sulfur cluster assembly
Chain IDs:A
Chain Length:106
Number of Molecules:1
Biological Source:Escherichia coli
Primary Citation
Comparative Structural Analysis of Escherichia Coli Cyay at Room and Cryogenic Temperatures Using Macromolecular and Serial Crystallography.
Chembiochem 26 e202500442 e202500442 (2025)
PMID: 41147201 DOI: 10.1002/cbic.202500442

Abstact

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.

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