CBS (cystathionin beta-synthase) Domain Protein TA0289 - A New Family

A modular protein mystery

Bioinformatics is "the collection, classification, storage, and analysis of biochemicals and biological information using computers especially as applied to molecular genetics and genomics."  (Merriam-Webster,2010 ) Research in bioinformatics shows many proteins are modular which means it can mix and match modules to form new proteins with new functions.
 All image credit is given to both David Goodsell and the PSI Structural Genomics Knowledgebase
Researchers at Protein Structure Initiative (PSI) Midwest Center for Structural Genomics (MCSG) http://www.mcsg.anl.gov/ are in the business to developing "integrated methods for highly cost-effective determination of protein structures through X-ray crystallography."  MCSG discovered this "new structure of a protein" and "made the first steps towards uncovering the function of this unusual new family of proteins" called CBS  Domain Protein TA0289.

MCSG uncovered several proteins that contained the CBS amino acid sequence. (w. Minor Lab, 2010)  These domains were "connected to a short unannotated sequence with four cysteine amino acids."  The "CBS module can add a regulatory function to a protein, changing activity of the protein based on the levels of ATP in the cell."  Along with affecting function, "CBS modules also play structural roles, by forming protein-protein interaction sites in oligomeric complexes."

  

The structure, after purification, revealed a reddish-purple color which led to a better understanding of TA0289's function. The color is a result of the metal-binding site being occupied by iron ions. If TA0289 could transport electrons then it could perform valuable functions within the cell. This discovery shows that "CBS domain links the two chains into a stable dimer, so its role may be primarily structural." 

"Why TA0289 needs to be a dimer is still a mystery."

 
Works Cited

Merriam-Webster. (2010). Merriam-Webster's Collegiate Dictionary, Eleventh Edition. Retrieved February 26, 2010, from Merriam-Webster Inc Web Site: http://www.merriam-webster.com/dictionary/bioinformatics

Proudfoot, M. S. (2008, January 4). Biochemical and Sturctural Characterization of a Novel Family of Cystationine Beta-Synthase Domain Fused to a Zn Ribbon-Like Domain. Retrieved February 26, 2010, from ScienceDirect - Journal of Molecular Biology Volumer 375, Issue 1: http://dx.doi.org/10.1016/j.jmb.2007.10.060


Goodsell, D. S. (2010, March). PSI-Nature Structural Genomics Knowledgebase. Retrieved February 26, 2010, from CBS Domain Protein TA0289 (ISSN 1758-1338): http://kb.psistructuralgenomics.org/KB/archives.jsp?pageshow=11


Rutgers and UCSD. (2010, March 2). RCSB Protein Data Bank (PDB). Retrieved February 26, 2010, from An Information Portal to Biological Macromolecular Structures: http://www.rcsb.org/pdb/results/results.do?outformat=&qrid=2BDCA0C9&tabtoshow=Current


W. Minor Lab. (2010). Midwest Center for Structural Genomics. Retrieved February 26, 2010, from MCSG: http://www.mcsg.anl.gov/