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3LWH

Crystal structure of Cren7-dsDNA complex

Summary for 3LWH
Entry DOI10.2210/pdb3lwh/pdb
Related3LWI
DescriptorChromatin protein Cren7, DNA (5'-D(*GP*TP*AP*AP*TP*TP*AP*C)-3') (3 entities in total)
Functional Keywordsprotein-dna complex, beta-sheet, dna-binding, methylation, dna binding protein-dna complex, dna binding protein/dna
Biological sourceSulfolobus solfataricus
Cellular locationCytoplasm (Probable): Q97ZE3
Total number of polymer chains3
Total formula weight11529.17
Authors
Zhang, Z.F.,Gong, Y.,Guo, L.,Jiang, T.,Huang, L. (deposition date: 2010-02-23, release date: 2010-05-26, Last modification date: 2023-11-01)
Primary citationZhang, Z.F.,Gong, Y.,Guo, L.,Jiang, T.,Huang, L.
Structural insights into the interaction of the crenarchaeal chromatin protein Cren7 with DNA
Mol.Microbiol., 76:749-759, 2010
Cited by
PubMed Abstract: Cren7, a newly found chromatin protein, is highly conserved in the Crenarchaeota. The protein shows higher affinity for double-stranded DNA than for single-stranded DNA, constrains negative DNA supercoils in vitro and is associated with genomic DNA in vivo. Here we report the crystal structures of the Cren7 protein from Sulfolobus solfataricus in complex with two DNA sequences. Cren7 binds in the minor groove of DNA and causes a single-step sharp kink in DNA (approximately 53 degrees) through the intercalation of the hydrophobic side chain of Leu28. Loop beta 3-beta 4 of Cren7 undergoes a significant conformational change upon binding of the protein to DNA, suggesting its critical role in the stabilization of the protein-DNA complex. The roles of DNA-contacting amino acid residues in stabilizing the Cren7-DNA interaction were examined by mutational analysis. Structural comparison of Cren7-DNA complexes with Sac7d-DNA complexes reveals significant differences between the two proteins in DNA binding surface, suggesting that Cren7 and Sul7d serve distinct functions in chromosomal organization.
PubMed: 20345658
DOI: 10.1111/j.1365-2958.2010.07136.x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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