1ozv
From Proteopedia
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| - | [[Image:1ozv.jpg|left|200px]] | + | [[Image:1ozv.jpg|left|200px]] |
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| - | '''Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy''' | + | {{Structure |
| + | |PDB= 1ozv |SIZE=350|CAPTION= <scene name='initialview01'>1ozv</scene>, resolution 2.65Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=LYS:LYSINE'>LYS</scene> and <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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OZV is a [ | + | 1OZV 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=1OZV OCA]. |
==Reference== | ==Reference== | ||
| - | Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT., Trievel RC, Flynn EM, Houtz RL, Hurley JH, Nat Struct Biol. 2003 Jul;10(7):545-52. PMID:[http:// | + | Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT., Trievel RC, Flynn EM, Houtz RL, Hurley JH, Nat Struct Biol. 2003 Jul;10(7):545-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12819771 12819771] |
[[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 13:17:52 2008'' |
Revision as of 11:17, 20 March 2008
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| , resolution 2.65Å | |||||||
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| Ligands: | and | ||||||
| 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 | ||||||
Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy
Overview
SET domain protein methyltransferases catalyze the transfer of methyl groups from the cofactor S-adenosylmethionine (AdoMet) to specific lysine residues of protein substrates, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex. The crystal structures of pea Rubisco large subunit methyltransferase (LSMT) in ternary complexes with either lysine or epsilon-N-methyllysine (MeLys) and the product S-adenosylhomocysteine (AdoHcy) were determined to resolutions of 2.65 and 2.55 A, respectively. The zeta-methyl group of MeLys is bound to the enzyme via carbon-oxygen hydrogen bonds that play a key role in catalysis. The methyl donor and acceptor are aligned in a linear geometry for S(N)2 nucleophilic transfer of the methyl group during catalysis. Differences in hydrogen bonding between the MeLys epsilon-amino group and Rubisco LSMT and SET7/9 explain why Rubisco LSMT generates multiply methylated Lys, wheras SET7/9 generates only MeLys.
About this Structure
1OZV is a Single protein structure of sequence from Pisum sativum. Full crystallographic information is available from OCA.
Reference
Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT., Trievel RC, Flynn EM, Houtz RL, Hurley JH, Nat Struct Biol. 2003 Jul;10(7):545-52. PMID:12819771[[Category: [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase]]
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