1mlv: Difference between revisions
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[[Image:1mlv.gif|left|200px]] | [[Image:1mlv.gif|left|200px]] | ||
'''Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase''' | {{Structure | ||
|PDB= 1mlv |SIZE=350|CAPTION= <scene name='initialview01'>1mlv</scene>, resolution 2.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> and <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MLV is a [ | 1MLV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MLV OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12372303 12372303] | ||
[[Category: Pisum sativum]] | [[Category: Pisum sativum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: set domain]] | [[Category: set domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:45:03 2008'' | ||
Revision as of 10:45, 20 March 2008
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| 1mlv, resolution 2.60Å | |||||||||||||
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| Ligands: | SAH and EPE | ||||||||||||
| Activity: | [Ribulose-bisphosphate_carboxylase-lysine_N-methyltransferase [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase], with EC number 2.1.1.127 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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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