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Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects
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SYSNO ASEP 0562970 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects Author(s) Adámková, Kristýna (BTO-N)
Koval, Tomáš (BTO-N) ORCID
Ostergaard, L. H. (DK)
Dušková, Jarmila (BTO-N) RID, SAI
Malý, Martin (BTO-N) ORCID
Švecová, Leona (BTO-N)
Skálová, Tereza (BTO-N) RID, ORCID
Kolenko, Petr (BTO-N) ORCID, RID
Dohnálek, Jan (BTO-N) RID, ORCIDNumber of authors 9 Source Title Acta Crystallographica Section D-Biological Crystallography. - : Oxford Blackwell - ISSN 1399-0047
Roč. 78, OCT 1 2022 (2022), s. 1194-1209Number of pages 16 s. Language eng - English Country DK - Denmark Keywords S1 nuclease ; Aspergillus oryzae ; lattice-translocation defects ; nucleotides ; nucleosides ; complexes Subject RIV CB - Analytical Chemistry, Separation OECD category Analytical chemistry R&D Projects LM2015043 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LM2018127 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA20-12109S GA ČR - Czech Science Foundation (CSF) EF15_003/0000447 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Limited access Institutional support BTO-N - RVO:86652036 UT WOS 000865745200002 EID SCOPUS 85139137906 DOI 10.1107/S2059798322008397 Annotation 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. Workplace Institute of Biotechnology Contact Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700 Year of Publishing 2023 Electronic address https://scripts.iucr.org/cgi-bin/paper?S2059798322008397
Number of the records: 1