1ozv
From Proteopedia
(New page: 200px<br /><applet load="1ozv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ozv, resolution 2.65Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ozv.jpg|left|200px]]<br /><applet load="1ozv" size=" | + | [[Image:1ozv.jpg|left|200px]]<br /><applet load="1ozv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ozv, resolution 2.65Å" /> | caption="1ozv, resolution 2.65Å" /> | ||
'''Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy'''<br /> | '''Crystal structure of the SET domain of LSMT bound to Lysine and AdoHcy'''<br /> | ||
==Overview== | ==Overview== | ||
| - | SET domain protein methyltransferases catalyze the transfer of methyl | + | 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== | ==About this Structure== | ||
| - | 1OZV 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 LYS and SAH 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:// | + | 1OZV 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=LYS:'>LYS</scene> and <scene name='pdbligand=SAH:'>SAH</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=1OZV OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase]] | [[Category: [Ribulose-bisphosphate carboxylase]-lysine N-methyltransferase]] | ||
| - | [[Category: Flynn, E | + | [[Category: Flynn, E M.]] |
| - | [[Category: Houtz, R | + | [[Category: Houtz, R L.]] |
| - | [[Category: Hurley, J | + | [[Category: Hurley, J H.]] |
| - | [[Category: Trievel, R | + | [[Category: Trievel, R C.]] |
[[Category: LYS]] | [[Category: LYS]] | ||
[[Category: SAH]] | [[Category: SAH]] | ||
| Line 26: | Line 26: | ||
[[Category: set domain]] | [[Category: set domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:32 2008'' |
Revision as of 12:23, 21 February 2008
|
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 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
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]]
Page seeded by OCA on Thu Feb 21 14:23:32 2008
