1mlv
From Proteopedia
(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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| - | [[Image:1mlv.gif|left|200px]]<br /><applet load="1mlv" size=" | + | [[Image:1mlv.gif|left|200px]]<br /><applet load="1mlv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mlv, resolution 2.60Å" /> | caption="1mlv, resolution 2.60Å" /> | ||
'''Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase'''<br /> | '''Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Protein lysine methylation by SET domain enzymes regulates chromatin | + | 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== | ==About this Structure== | ||
| - | 1MLV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with SAH and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/[Ribulose-bisphosphate_carboxylase]-lysine_N-methyltransferase [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.127 2.1.1.127] Full crystallographic information is available from [http:// | + | 1MLV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with <scene name='pdbligand=SAH:'>SAH</scene> and <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/[Ribulose-bisphosphate_carboxylase]-lysine_N-methyltransferase [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.127 2.1.1.127] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MLV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase]] | [[Category: [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase]] | ||
| - | [[Category: Beach, B | + | [[Category: Beach, B M.]] |
| - | [[Category: Dirk, L | + | [[Category: Dirk, L M.A.]] |
| - | [[Category: Houtz, R | + | [[Category: Houtz, R L.]] |
| - | [[Category: Hurley, J | + | [[Category: Hurley, J H.]] |
| - | [[Category: Trievel, R | + | [[Category: Trievel, R C.]] |
[[Category: EPE]] | [[Category: EPE]] | ||
[[Category: SAH]] | [[Category: SAH]] | ||
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[[Category: set domain]] | [[Category: set domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:31 2008'' |
Revision as of 11:56, 21 February 2008
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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 and 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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