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Updated: Jul 10, 2026

Single-cell Analysis of Bacillus subtilis Biofilms Using Fluorescence Microscopy and Flow Cytometry

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Published on: February 15, 2012

Crystal structure of Bacillus subtilis YckF: structural and functional evolution.

R Sanishvili¹, R Wu, D E Kim

¹Structural Biology Center, Biosciences Division, Argonne National Laboratory, 9700 South Cass Avenue, Building 202, IL 60439, USA.

Journal of Structural Biology

|September 15, 2004

Summary

The crystal structure of Bacillus subtilis YckF protein reveals a tetrameric form, crucial for its phosphate sugar isomerase activity. This oligomerization is conserved, suggesting physiological relevance and potential insights into gene evolution.

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Area of Science:

Biochemistry
Structural Biology
Enzymology

Background:

The YckF protein from Bacillus subtilis is a phosphate sugar isomerase.
Understanding its structure and function is key to comprehending metabolic pathways.

Purpose of the Study:

To determine the crystal structure of the YckF protein.
To investigate its oligomerization state and compare it with related proteins.
To identify residues involved in substrate binding and catalysis.

Main Methods:

X-ray crystallography with MAD phasing.
Protein structure determination and refinement at 1.95Å resolution.
Sequence and structural comparisons with orthologs and related enzymes.

Main Results:

The crystal structure of YckF was determined, revealing a stable tetrameric quaternary structure in both crystalline and solution states.
Structural comparison with Methanococcus jannaschii MJ1247 and Escherichia coli glucosamine-6-phosphate synthase identified conserved residues for substrate binding and catalysis.
Differences in active sites suggest potential cooperativity within the tetramer.

Conclusions:

The tetrameric structure of YckF is physiologically relevant for its phosphate hexulose isomerase activity.
Structural insights provide a basis for understanding enzyme mechanism and evolution.
Phylogenetic analysis offers clues into the evolutionary adaptation of genes in methylotrophic organisms.