1p91

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spinqualitylabelsall models 1p91, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of RlmA(I) enzyme: 23S rRNA n1-G745 methyltransferase (NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET ER19)

Overview

The RlmA class of enzymes (RlmA(I) and RlmA(II)) catalyzes N1-methylation, of a guanine base (G745 in Gram-negative and G748 in Gram-positive, bacteria) of hairpin 35 of 23S rRNA. We have determined the crystal, structure of Escherichia coli RlmA(I) at 2.8-A resolution, providing 3D, structure information for the RlmA class of RNA methyltransferases. The, dimeric protein structure exhibits features that provide new insights into, its molecular function. Each RlmA(I) molecule has a Zn-binding domain, responsible for specific recognition and binding of its rRNA substrate, and a methyltransferase domain. The asymmetric RlmA(I) dimer observed in, the crystal structure has a well defined W-shaped RNA-binding cleft. Two, S-adenosyl-l-methionine substrate molecules are located at the two valleys, of the W-shaped RNA-binding cleft. The unique shape of the RNA-binding, cleft, different from that of known RNA-binding proteins, is highly, specific and structurally complements the 3D structure of hairpin 35 of, bacterial 23S rRNA. Apart from the hairpin 35, parts of hairpins 33 and 34, also interact with the RlmA(I) dimer.

About this Structure

1P91 is a Single protein structure of sequence from Escherichia coli with ZN, SO4 and SAM as ligands. Active as rRNA (guanine-N(1)-)-methyltransferase, with EC number 2.1.1.51 Full crystallographic information is available from OCA.

Reference

Crystal structure of RlmAI: implications for understanding the 23S rRNA G745/G748-methylation at the macrolide antibiotic-binding site., Das K, Acton T, Chiang Y, Shih L, Arnold E, Montelione GT, Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4041-6. Epub 2004 Mar 3. PMID:14999102

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