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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 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects Tvůrce(i) 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, ORCIDCelkový počet autorů 9 Zdroj.dok. Acta Crystallographica Section D-Biological Crystallography. - : Oxford Blackwell - ISSN 1399-0047
Roč. 78, OCT 1 2022 (2022), s. 1194-1209Poč.str. 16 s. Jazyk dok. eng - angličtina Země vyd. DK - Dánsko Klíč. slova S1 nuclease ; Aspergillus oryzae ; lattice-translocation defects ; nucleotides ; nucleosides ; complexes Vědní obor RIV CB - Analytická chemie, separace Obor OECD Analytical chemistry CEP LM2015043 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy LM2018127 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GA20-12109S GA ČR - Grantová agentura ČR EF15_003/0000447 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Omezený přístup Institucionální podpora BTO-N - RVO:86652036 UT WOS 000865745200002 EID SCOPUS 85139137906 DOI 10.1107/S2059798322008397 Anotace 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. Pracoviště Biotechnologický ústav Kontakt Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700 Rok sběru 2023 Elektronická adresa https://scripts.iucr.org/cgi-bin/paper?S2059798322008397
Počet záznamů: 1