Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F22%3A00128763" target="_blank" >RIV/00216224:14740/22:00128763 - isvavai.cz</a>

Alternative codes found

RIV/68407700:21340/22:00363905

Result on the web

<a href="https://scripts.iucr.org/cgi-bin/paper?S2059798322008397" target="_blank" >https://scripts.iucr.org/cgi-bin/paper?S2059798322008397</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S2059798322008397" target="_blank" >10.1107/S2059798322008397</a>

Result language

angličtina

Original language name

Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

—

Continuities

—

Publication year

2022

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Acta Crystallographica Section D: Structural Biology

ISSN

2059-7983

e-ISSN

—

Volume of the periodical

78

Issue of the periodical within the volume

OCT

Country of publishing house

GB - UNITED KINGDOM

Number of pages

16

Pages from-to

1194-1209

UT code for WoS article

000865745200002

EID of the result in the Scopus database

2-s2.0-85139137906