5xj1

Crystal structure of spRlmCD

spinqualitylabelsall models 5xj1, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xj1 is a 1 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.753Å Ligands: EPE, GOL, P6G Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Y1029_STRPN Publication Abstract from PubMed RlmCD has recently been identified as the S-adenosyl methionine (SAM)-dependent methyltransferase responsible for the formation of m5U at U747 and U1939 of 23S ribosomal RNA in Streptococcus pneumoniae. In this research, we determine the high-resolution crystal structures of apo-form RlmCD and its complex with SAH. Using an in-vitro methyltransferase assay, we reveal the crucial residues for its catalytic functions. Furthermore, structural comparison between RlmCD and its structural homologue RumA, which only catalyzes the m5U1939 in Escherichia coli, implicates that a unique long linker in the central domain of RlmCD is the key factor in determining its substrate selectivity. Its significance in the enzyme activity of RlmCD is further confirmed by in-vitro methyltransferase assay. Structural insights into substrate selectivity of ribosomal RNA methyltransferase RlmCD.,Jiang Y, Li F, Wu J, Shi Y, Gong Q PLoS One. 2017 Sep 26;12(9):e0185226. doi: 10.1371/journal.pone.0185226., eCollection 2017. PMID:28949991 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA