1orh
From Proteopedia
(New page: 200px<br /><applet load="1orh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1orh, resolution 2.64Å" /> '''Structure of the Pre...) |
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| - | [[Image:1orh.gif|left|200px]]<br /><applet load="1orh" size=" | + | [[Image:1orh.gif|left|200px]]<br /><applet load="1orh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1orh, resolution 2.64Å" /> | caption="1orh, resolution 2.64Å" /> | ||
'''Structure of the Predominant Protein Arginine Methyltransferase PRMT1'''<br /> | '''Structure of the Predominant Protein Arginine Methyltransferase PRMT1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | PRMT1 is the predominant type I protein arginine methyltransferase in | + | PRMT1 is the predominant type I protein arginine methyltransferase in mammals and highly conserved among all eukaryotes. It is essential for early postimplantation development in mouse. Here we describe the crystal structure of rat PRMT1 in complex with the reaction product AdoHcy and a 19 residue substrate peptide containing three arginines. The results reveal a two-domain structure-an AdoMet binding domain and a barrel-like domain-with the active site pocket located between the two domains. Mutagenesis studies confirmed that two active site glutamates are essential for enzymatic activity, and that dimerization of PRMT1 is essential for AdoMet binding. Three peptide binding channels are identified: two are between the two domains, and the third is on the surface perpendicular to the strands forming the beta barrel. |
==About this Structure== | ==About this Structure== | ||
| - | 1ORH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SAH and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Histone-arginine_N-methyltransferase Histone-arginine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.125 2.1.1.125] Full crystallographic information is available from [http:// | + | 1ORH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SAH:'>SAH</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Histone-arginine_N-methyltransferase Histone-arginine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.125 2.1.1.125] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ORH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein arginine methylation adomet-dependent methylation]] | [[Category: protein arginine methylation adomet-dependent methylation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:46 2008'' |
Revision as of 12:20, 21 February 2008
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Structure of the Predominant Protein Arginine Methyltransferase PRMT1
Overview
PRMT1 is the predominant type I protein arginine methyltransferase in mammals and highly conserved among all eukaryotes. It is essential for early postimplantation development in mouse. Here we describe the crystal structure of rat PRMT1 in complex with the reaction product AdoHcy and a 19 residue substrate peptide containing three arginines. The results reveal a two-domain structure-an AdoMet binding domain and a barrel-like domain-with the active site pocket located between the two domains. Mutagenesis studies confirmed that two active site glutamates are essential for enzymatic activity, and that dimerization of PRMT1 is essential for AdoMet binding. Three peptide binding channels are identified: two are between the two domains, and the third is on the surface perpendicular to the strands forming the beta barrel.
About this Structure
1ORH is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Active as Histone-arginine N-methyltransferase, with EC number 2.1.1.125 Full crystallographic information is available from OCA.
Reference
Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides., Zhang X, Cheng X, Structure. 2003 May;11(5):509-20. PMID:12737817
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