4m37 | pdb_00004m37

Crystal structure of Trypanosoma brucei protein arginine methyltransferase 7 complex with AdoHcy

spinqualitylabelsall models 4m37, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4m37 is a 1 chain structure with sequence from Tryb2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SAH Related: 4m36, 4m38 Gene: PRMT7, Tb927.7.5490 (TRYB2) Resources: FirstGlance, OCA, RCSB, PDBsum Function [ANM7_TRYB2] Arginine methyltransferase that specifically catalyzes the formation of omega-N monomethylarginine (MMA). Has activity toward multiple substrates in vitro. Able to mediate the arginine methylation of histones and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo. Publication Abstract from PubMed Trypanosoma brucei protein arginine methyltransferase 7 (TbPRMT7) exclusively generates monomethylarginine (MMA), which directs biological consequences distinct from that of symmetric dimethylarginine (SDMA) and asymmetric dimethylarginine (ADMA). However, determinants controlling the strict monomethylation activity are unknown. We present the crystal structure of the TbPRMT7 active core in complex with S-adenosyl-L-homocysteine (AdoHcy) and a histone H4 peptide substrate. In the active site, residues E172, E181, and Q329 hydrogen bond the guanidino group of the target arginine and align the terminal guanidino nitrogen in a position suitable for nucleophilic attack on the methyl group of S-adenosyl-L-methionine (AdoMet). Structural comparisons and isothermal titration calorimetry data suggest that the TbPRMT7 active site is narrower than those of protein arginine dimethyltransferases, making it unsuitable to bind MMA in a manner that would support a second turnover, thus abolishing the production of SDMA and ADMA. Our results present the structural interpretations for the monomethylation activity of TbPRMT7. Structural Determinants for the Strict Monomethylation Activity by Trypanosoma brucei Protein Arginine Methyltransferase 7.,Wang C, Zhu Y, Caceres TB, Liu L, Peng J, Wang J, Chen J, Chen X, Zhang Z, Zuo X, Gong Q, Teng M, Hevel JM, Wu J, Shi Y Structure. 2014 Apr 8. pii: S0969-2126(14)00075-6. doi:, 10.1016/j.str.2014.03.003. PMID:24726341 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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