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1zkk
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> | |LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span> |
|GENE= SET8, PRSET7, SET07 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SET8, PRSET7, SET07 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zkk OCA], [http://www.ebi.ac.uk/pdbsum/1zkk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zkk RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Couture, J F.]] | [[Category: Couture, J F.]] | ||
[[Category: Trievel, R C.]] | [[Category: Trievel, R C.]] | ||
| - | [[Category: SAH]] | ||
[[Category: beta-sheet]] | [[Category: beta-sheet]] | ||
[[Category: histone h4]] | [[Category: histone h4]] | ||
[[Category: pseudo-knot]] | [[Category: pseudo-knot]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:37:57 2008'' |
Revision as of 22:37, 30 March 2008
| |||||||
| , resolution 1.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | SET8, PRSET7, SET07 (Homo sapiens) | ||||||
| Activity: | Histone-lysine N-methyltransferase, with EC number 2.1.1.43 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy
Overview
SET8 (also known as PR-SET7) is a histone H4-Lys-20-specific methyltransferase that is implicated in cell-cycle-dependent transcriptional silencing and mitotic regulation in metazoans. Herein we report the crystal structure of human SET8 (hSET8) bound to a histone H4 peptide bearing Lys-20 and the product cofactor S-adenosylhomocysteine. Histone H4 intercalates in the substrate-binding cleft as an extended parallel beta-strand. Residues preceding Lys-20 in H4 engage in an extensive array of salt bridge, hydrogen bond, and van der Waals interactions with hSET8, while the C-terminal residues bind through predominantly hydrophobic interactions. Mutational analysis of both the substrate-binding cleft and histone H4 reveals that interactions with residues in the N and C termini of the H4 peptide are critical for conferring substrate specificity. Finally, analysis of the product specificity indicates that hSET8 is a monomethylase, consistent with its role in the maintenance of Lys-20 monomethylation during cell division.
About this Structure
1ZKK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase., Couture JF, Collazo E, Brunzelle JS, Trievel RC, Genes Dev. 2005 Jun 15;19(12):1455-65. Epub 2005 Jun 2. PMID:15933070
Page seeded by OCA on Mon Mar 31 01:37:57 2008
