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4QEP

crystal structure of KRYPTONITE in complex with mCHG DNA and SAH

Summary for 4QEP
Entry DOI10.2210/pdb4qep/pdb
Related4QEN 4QEO
DescriptorHistone-lysine N-methyltransferase, H3 lysine-9 specific SUVH4, DNA (5'-D(*GP*GP*TP*AP*CP*TP*(5CM)P*AP*GP*CP*AP*GP*TP*AP*T)-3'), DNA (5'-D(*AP*CP*TP*GP*CP*TP*GP*AP*GP*TP*AP*CP*CP*AP*T)-3'), ... (5 entities in total)
Functional Keywordssra, set, histone methylation, methylated dna, methylation, transcription-dna complex, transcription/dna
Biological sourceArabidopsis thaliana (mouse-ear cress,thale-cress)
Cellular locationNucleus: Q8GZB6
Total number of polymer chains3
Total formula weight69524.87
Authors
Du, J.,Li, S.,Patel, D.J. (deposition date: 2014-05-17, release date: 2014-07-30, Last modification date: 2023-09-20)
Primary citationDu, J.,Johnson, L.M.,Groth, M.,Feng, S.,Hale, C.J.,Li, S.,Vashisht, A.A.,Gallego-Bartolome, J.,Wohlschlegel, J.A.,Patel, D.J.,Jacobsen, S.E.
Mechanism of DNA Methylation-Directed Histone Methylation by KRYPTONITE.
Mol.Cell, 55:495-504, 2014
Cited by
PubMed Abstract: In Arabidopsis, CHG DNA methylation is controlled by the H3K9 methylation mark through a self-reinforcing loop between DNA methyltransferase CHROMOMETHYLASE3 (CMT3) and H3K9 histone methyltransferase KRYPTONITE/SUVH4 (KYP). We report on the structure of KYP in complex with methylated DNA, substrate H3 peptide, and cofactor SAH, thereby defining the spatial positioning of the SRA domain relative to the SET domain. The methylated DNA is bound by the SRA domain with the 5mC flipped out of the DNA, while the H3(1-15) peptide substrate binds between the SET and post-SET domains, with the ε-ammonium of K9 positioned adjacent to bound SAH. These structural insights, complemented by functional data on key mutants of residues lining the 5mC and H3K9-binding pockets within KYP, establish how methylated DNA recruits KYP to the histone substrate. Together, the structures of KYP and previously reported CMT3 complexes provide insights into molecular mechanisms linking DNA and histone methylation.
PubMed: 25018018
DOI: 10.1016/j.molcel.2014.06.009
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

227344

數據於2024-11-13公開中

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