Evidence map›Paper›PMID 33877576›Full record

ArticleJournal of microbiology (Seoul, Korea)2021

Crystal structure of the nuclease and capping domain of SbcD from Staphylococcus aureus.

Jinwook Lee, Inseong Jo, Jinsook Ahn, Seokho Hong, Soyeon Jeong, Aeran Kwon, Nam-Chul Ha

Abstract read
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In one paragraph

Article in Journal of microbiology (Seoul, Korea), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 52% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 6 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Jinwook LeeResearch Institute of Agriculture and Life Sciences, Center for Food and Bioconvergence, Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul, 08826, Republic of Korea.
Inseong JoResearch Institute of Agriculture and Life Sciences, Center for Food and Bioconvergence, Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul, 08826, Republic of Korea.
Jinsook AhnResearch Institute of Agriculture and Life Sciences, Center for Food and Bioconvergence, Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul, 08826, Republic of Korea.
Seokho HongResearch Institute of Agriculture and Life Sciences, Center for Food and Bioconvergence, Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul, 08826, Republic of Korea.
Soyeon JeongResearch Institute of Agriculture and Life Sciences, Center for Food and Bioconvergence, Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul, 08826, Republic of Korea.
Aeran KwonDepartment of Beauty Care, College of Medical Science, Daegu Haany University, Gyeongsan, 38610, Republic of Korea.
Nam-Chul HaResearch Institute of Agriculture and Life Sciences, Center for Food and Bioconvergence, Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul, 08826, Republic of Korea. hanc210@snu.ac.kr.
Seoul National University · KRDaegu Haany University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SbcCD complex is an essential component of the DNA double-strand break (DSB) repair system in bacteria. The bacterial SbcCD complex recognizes and cleaves the DNA ends in DSBs by ATP-dependent endo- and exonuclease activities as an early step of the DNA repair process. SbcD consists of nuclease, capping, and helix-loop-helix domains. Here, we present the crystal structure of a SbcD fragment from Staphylococcus aureus, which contained nuclease and capping domains, at a resolution of 2.9 Å. This structure shows a dimeric assembly similar to that of the corresponding domains of SbcD from Escherichia coli. The S. aureus SbcD fragment exhibited endonuclease activities on supercoiled DNA and exonuclease activity on linear and nicked DNA. This study contributes to the understanding of the molecular basis for how bacteria can resist sterilizing treatment, causing DNA damage.

Indexed as

Bacterial ProteinsCatalytic DomainCrystallizationDeoxyribonucleasesDNA, BacterialDNA Breaks, Double-StrandedDNA RepairEscherichia coliProtein ConformationProtein DomainsStaphylococcus aureusBacterial ProteinsDeoxyribonucleasesDNA, Bacterialcrystal structureDNA double strand breakageDNA repairnucleaseSbcDStaphylococcus aureus

Identifiers

PMID33877576
OpenAlexW3154942141

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.