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Crystal structure of the crenarchaeal conserved chromatin protein Cren7 and double-stranded DNA complex.

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Crystal structure of the crenarchaeal conserved chromatin protein Cren7 and double-stranded DNA complex.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Feng, Yingang Yao, Hongwei Wang, Jinfeng
Description	Author Affiliation: Feng Y ( National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.)
Abstract	Cren7 is a crenarchaeal conserved chromatin protein discovered recently. To explore the mechanism of the DNA packaging in Crenarchaeota, the crystal structure of Cren7-GCGATCGC complex has been determined and refined at 1.6 A resolution. Cren7 kinks the dsDNA sharply similar to Sul7d, another chromatin protein existing only in Sulfolobales, which reveals that the 'bending and unwinding' compacting mechanism is conserved in Crenarchaeota. Significant structural differences are revealed by comparing both protein-dsDNA complexes. The kinked sites on the same dsDNA in the complexes with Sul7d and Cren7 show one base pair shift. For Cren7, fewer charged residues in the beta-barrel structural region bind to DNA, and additionally, the flexible loop L(beta3beta4) is also involved in the binding. Electrophoretic mobility shift assays indicate that loop L(beta3beta4) is essential for DNA-binding of Cren7. These differences provide insight into the functional difference of both chromatin proteins, suggesting that Cren7 may be more regulative than Sul7d in the DNA-binding affinity by the methylation in the flexible loop L(beta3beta4) in vivo.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1002/pro.385
Journal	Protein Science
Issue Number	6
Volume Number	19
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2010-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Archaeal Proteins Chemistry Chromosomal Proteins, Non-histone Crenarchaeota Metabolism Crystallography, X-ray Dna-binding Proteins Nuclear Magnetic Resonance, Biomolecular Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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