1oyp
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(New page: 200px<br /><applet load="1oyp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oyp, resolution 2.76Å" /> '''Crystal Structure of...)
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Revision as of 21:10, 20 November 2007
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Crystal Structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis
Overview
RNase PH is a member of the family of phosphorolytic 3' --> 5', exoribonucleases that also includes polynucleotide phosphorylase (PNPase)., RNase PH is involved in the maturation of tRNA precursors and especially, important for removal of nucleotide residues near the CCA acceptor end of, the mature tRNAs. Wild-type and triple mutant R68Q-R73Q-R76Q RNase PH from, Bacillus subtilis have been crystallized and the structures determined by, X-ray diffraction to medium resolution. Wild-type and triple mutant RNase, PH crystallize as a hexamer and dimer, respectively. The structures, contain a rare left-handed beta alpha beta-motif in the N-terminal portion, of the protein. This motif has also been identified in other enzymes, involved in RNA metabolism. The RNase PH structure and active site can, despite low sequence similarity, be overlayed with the N-terminal core of, the structure and active site of Streptomyces antibioticus PNPase. The, surface of the RNase PH dimer fit the shape of a tRNA molecule.
About this Structure
1OYP is a Single protein structure of sequence from Bacillus subtilis with SO4 as ligand. Active as tRNA nucleotidyltransferase, with EC number 2.7.7.56 Full crystallographic information is available from OCA.
Reference
Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding., Harlow LS, Kadziola A, Jensen KF, Larsen S, Protein Sci. 2004 Mar;13(3):668-77. Epub 2004 Feb 6. PMID:14767080
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