2bqz

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|PDB= 2bqz |SIZE=350|CAPTION= <scene name='initialview01'>2bqz</scene>, resolution 1.50&Aring;
|PDB= 2bqz |SIZE=350|CAPTION= <scene name='initialview01'>2bqz</scene>, resolution 1.50&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>
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|LIGAND= <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>
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|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]
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|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=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bqz OCA], [http://www.ebi.ac.uk/pdbsum/2bqz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bqz RCSB]</span>
}}
}}
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[[Category: Wilson, J R.]]
[[Category: Wilson, J R.]]
[[Category: Xiao, B.]]
[[Category: Xiao, B.]]
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[[Category: SAH]]
 
[[Category: histone h4 methyltransfersae]]
[[Category: histone h4 methyltransfersae]]
[[Category: lysine methyltransferase]]
[[Category: lysine methyltransferase]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:05:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:10:25 2008''

Revision as of 23:10, 30 March 2008

Image:2bqz.gif


PDB ID 2bqz

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands: ,
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 A TERNARY COMPLEX OF THE HUMAN HISTONE METHYLTRANSFERASE PR-SET7 (ALSO KNOWN AS SET8)


Overview

Methylation of lysine residues of histones is an important epigenetic mark that correlates with functionally distinct regions of chromatin. We present here the crystal structure of a ternary complex of the enzyme Pr-Set7 (also known as Set8) that methylates Lys 20 of histone H4 (H4-K20). We show that the enzyme is exclusively a mono-methylase and is therefore responsible for a signaling role quite distinct from that established by other enzymes that target this histone residue. We provide evidence from NMR for the C-flanking domains of SET proteins becoming ordered upon addition of AdoMet cofactor and develop a model for the catalytic cycle of these enzymes. The crystal structure reveals the basis of the specificity of the enzyme for H4-K20 because a histidine residue within the substrate, close to the target lysine, is required for completion of the active site. We also show how a highly variable component of the SET domain is responsible for many of the enzymes' interactions with its target histone peptide and probably also how this part of the structure ensures that Pr-Set7 is nucleosome specific.

About this Structure

2BQZ is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Specificity and mechanism of the histone methyltransferase Pr-Set7., Xiao B, Jing C, Kelly G, Walker PA, Muskett FW, Frenkiel TA, Martin SR, Sarma K, Reinberg D, Gamblin SJ, Wilson JR, Genes Dev. 2005 Jun 15;19(12):1444-54. Epub 2005 Jun 2. PMID:15933069

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