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Streptococcus pneumonia YlxR at 1.35 A shows a putative new fold
1Argonne National Laboratory, Structural Biology Center, Biosciences Division, IL 60439, USA.
Acta Crystallographica. Section D, Biological Crystallography
|October 27, 2001
Summary
The YlxR protein from Streptococcus pneumonia has a novel structure, suggesting it may bind to RNA. This finding opens new avenues for understanding bacterial protein functions.
Area of Science:
- Structural Biology
- Biochemistry
- Microbiology
Background:
- The YlxR protein from Streptococcus pneumonia has an unknown function.
- YlxR belongs to a conserved protein family (COG2740) with a GRGA(Y/W) motif.
- No significant sequence or structural homology exists with known proteins.
Purpose of the Study:
- To determine the three-dimensional structure of the YlxR protein.
- To investigate the potential function of YlxR based on its structural characteristics.
Main Methods:
- High-resolution (1.35 Å) X-ray crystallography was employed.
- Three-wavelength anomalous dispersion (MAD) data were collected using synchrotron radiation.
- Structure determination utilized a semi-automated approach.
Main Results:
- The YlxR structure reveals a novel alpha-beta plait fold, resembling a two-layer sandwich.
- A prominent positively charged surface patch suggests potential nucleic acid binding.
- Analysis identified extensive clefts, including one spanning 3/4 of the protein, similar to RNA-binding proteins.
Conclusions:
- YlxR represents a new protein fold within the alpha-beta plait superfamily.
- Structural features strongly suggest YlxR functions as an RNA-binding protein.
- This discovery provides insights into bacterial protein families with conserved motifs.