1mlv: Difference between revisions

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[[Image:1mlv.gif|left|200px]]
{{Seed}}
[[Image:1mlv.png|left|200px]]


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{{STRUCTURE_1mlv|  PDB=1mlv  |  SCENE=  }}  
{{STRUCTURE_1mlv|  PDB=1mlv  |  SCENE=  }}  


'''Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase'''
===Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase===




==Overview==
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Protein lysine methylation by SET domain enzymes regulates chromatin structure, gene silencing, transcriptional activation, plant metabolism, and other processes. The 2.6 A resolution structure of Rubisco large subunit methyltransferase in a pseudo-bisubstrate complex with S-adenosylhomocysteine and a HEPES ion reveals an all-beta architecture for the SET domain embedded within a larger alpha-helical enzyme fold. Conserved regions of the SET domain bind S-adenosylmethionine and substrate lysine at two sites connected by a pore. We propose that methyl transfer is catalyzed by a conserved Tyr at a narrow pore connecting the sites. The cofactor enters by a "back door" on the opposite side of the enzyme from substrate, promoting highly specific protein recognition and allowing addition of multiple methyl groups.
The line below this paragraph, {{ABSTRACT_PUBMED_12372303}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12372303 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12372303}}


==About this Structure==
==About this Structure==
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[[Category: Post-translational modification]]
[[Category: Post-translational modification]]
[[Category: Set domain]]
[[Category: Set domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:23:49 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:17:34 2008''
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