1mlv: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1mlv.gif|left|200px]]<br /><applet load="1mlv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1mlv, resolution 2.60&Aring;" />
caption="1mlv, resolution 2.60&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MLV OCA].  
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.M.]]
[[Category: Beach, B M.]]
[[Category: Dirk, L.M.A.]]
[[Category: Dirk, L M.A.]]
[[Category: Houtz, R.L.]]
[[Category: Houtz, R L.]]
[[Category: Hurley, J.H.]]
[[Category: Hurley, J H.]]
[[Category: Trievel, R.C.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:31:00 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:31 2008''