1mlv
From Proteopedia
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|PDB= 1mlv |SIZE=350|CAPTION= <scene name='initialview01'>1mlv</scene>, resolution 2.60Å | |PDB= 1mlv |SIZE=350|CAPTION= <scene name='initialview01'>1mlv</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mlv OCA], [http://www.ebi.ac.uk/pdbsum/1mlv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mlv RCSB]</span> | ||
}} | }} | ||
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[[Category: Hurley, J H.]] | [[Category: Hurley, J H.]] | ||
[[Category: Trievel, R C.]] | [[Category: Trievel, R C.]] | ||
| - | [[Category: EPE]] | ||
| - | [[Category: SAH]] | ||
[[Category: lysine n-methylation]] | [[Category: lysine n-methylation]] | ||
[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
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[[Category: set domain]] | [[Category: set domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:17:52 2008'' |
Revision as of 19:17, 30 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | [Ribulose-bisphosphate_carboxylase-lysine_N-methyltransferase [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase], with EC number 2.1.1.127 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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]]
Page seeded by OCA on Sun Mar 30 22:17:52 2008
