7qtb

S1 nuclease from Aspergillus oryzae in complex with cytidine-5'-monophosphate

spinqualitylabelsall models 7qtb, resolution 1.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7qtb is a 2 chain structure with sequence from Aspergillus oryzae RIB40. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.04Å Ligands: BTB, C5P, CA, NAG, PO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NUS1_ASPOR Hydrolyzes only single-stranded DNA and RNA without apparent specificity for bases. Publication Abstract from PubMed S1 nuclease from Aspergillus oryzae is a single-strand-specific nuclease from the S1/P1 family that is utilized in biochemistry and biotechnology. S1 nuclease is active on both RNA and DNA but with differing catalytic efficiencies. This study clarifies its catalytic properties using a thorough comparison of differences in the binding of RNA and DNA in the active site of S1 nuclease based on X-ray structures, including two newly solved complexes of S1 nuclease with the products of RNA cleavage at atomic resolution. Conclusions derived from this comparison are valid for the whole S1/P1 nuclease family. For proper model building and refinement, multiple lattice-translocation defects present in the measured diffraction data needed to be solved. Two different approaches were tested and compared. Correction of the measured intensities proved to be superior to the use of the dislocation model of asymmetric units with partial occupancy of individual chains. As the crystals suffered from multiple lattice translocations, equations for their correction were derived de novo. The presented approach to the correction of multiple lattice-translocation defects may help to solve similar problems in the field of protein X-ray crystallography. Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects.,Adamkova K, Koval' T, Ostergaard LH, Duskova J, Maly M, Svecova L, Skalova T, Kolenko P, Dohnalek J Acta Crystallogr D Struct Biol. 2022 Oct 1;78(Pt 10):1194-1209. doi: , 10.1107/S2059798322008397. Epub 2022 Sep 27. PMID:36189740 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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