NDLI: Solution structure of ribosomal protein L40E, a unique C4 zinc finger protein encoded by archaeon Sulfolobus solfataricus.

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Solution structure of ribosomal protein L40E, a unique C4 zinc finger protein encoded by archaeon Sulfolobus solfataricus.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lemak, Alexander Semesi, Anthony Lukin, Jonathan Wu, Bin Arrowsmith, Cheryl H. Ramelot, Theresa A. Yee, Adelinda Kennedy, Michael A.
Description	Country affiliation: Canada Author Affiliation: Wu B ( Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, Toronto, Ontario M5G 2M9, Canada.)
Abstract	The ribosomal protein L40E from archaeon Sulfolobus solfataricus is a component of the 50S ribosomal subunit. L40E is a 56-residue, highly basic protein that contains a C4 zinc finger motif, CRKC_X(10)_CRRC. Homologs are found in both archaea and eukaryotes but are not present in bacteria. Eukaryotic genomes encode L40E as a ubiquitin-fusion protein. L40E was absent from the crystal structure of euryarchaeota 50S ribosomal subunit. Here we report the three-dimensional solution structure of L40E by NMR spectroscopy. The structure of L40E is a three-stranded beta-sheet with a simple beta2beta1beta3 topology. There are two unique characteristics revealed by the structure. First, a large and ordered beta2-beta3 loop twists to pack across the one side of the protein. L40E contains a buried polar cluster comprising Lys19, Lys20, Cys22, Asn29, and Cys36. Second, the surface of L40E is almost entirely positively charged. Ten conserved basic residues are positioned on the two sides of the surface. It is likely that binding of zinc is essential in stabilizing the tertiary structure of L40E to act as a scaffold to create a broad positively charged surface for RNA and/or protein recognition.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1110/ps.073273008
Journal	Protein Science
Issue Number	3
Volume Number	17
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2008-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Archaeal Proteins Chemistry Models, Molecular Ribosomal Proteins Sulfolobus Solfataricus Amino Acid Sequence Physiology Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Folding Sequence Alignment Zinc Metabolism Zinc Fingers Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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