1mlv
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(New page: 200px<br /><applet load="1mlv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mlv, resolution 2.60Å" /> '''Structure and Cataly...)
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Revision as of 19:23, 20 November 2007
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Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase
Overview
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.
About this Structure
1MLV is a Single protein structure of sequence from Pisum sativum with SAH and EPE as ligands. Active as [Ribulose-bisphosphate_carboxylase-lysine_N-methyltransferase [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase], with EC number 2.1.1.127 Full crystallographic information is available from OCA.
Reference
Structure and catalytic mechanism of a SET domain protein methyltransferase., Trievel RC, Beach BM, Dirk LM, Houtz RL, Hurley JH, Cell. 2002 Oct 4;111(1):91-103. PMID:12372303[[Category: [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase]]
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